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Trypsin References

Source:
Bovine Pancreas
CAS:
9002-07-7
EC:
3.4.21.4
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Abita, J. and Lazdunski, M.
On the Structural and Functional Role of Carboxylates in Chymotrypsinogen A: A Comparison with Chymotrypsin, Trypsinogen and Trypsin ,
Biochem Biophys Res Commun
 35 , 707 , 1969
Abuchowski, A. and Davis, F.
Preparation and Properties of Polyethylene Glycol-Trypsin Adducts ,
Biochim Biophys Acta
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Alagiri, S. and Singh, T.
Stability and Kinetics of a Bifunctional Amylase/ Trypsin Inhibitor ,
Biochim Biophys Acta
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Antonini, E. and Ascenzi, P.
The Mechanism of Trypsin Catalysis at Low pH. Proposal for a Structural Model ,
J Biol Chem
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Appavou, M. , Gibrat, G. and Bellissent-Funel, M.
Temperature Dependence on Structure and Dynamics of Bovine Pancreatic Trypsin Inhibitor (BPTI) A Neutron Scattering Study ,
Biochim Biophys Acta
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Arakawa, T. , Hung, L. , McGinley, M. , Rohde, M. and Narhi, L.
Induced Resistance of Trypsin to Sodium Dodecylsulfate upon Complex Formation with Trypsin Inhibitor ,
J Protein Chem
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Arentoft, A. , Frokiaer, H. , Michaelsen, S. , Sorensen, H. and Sorensen, S.
High-performance Capillary Electrophoresis for the Determination of Trypsin and Chymotrypsin Inhibitors and Their Association with Trypsin, Chymotrypsin and Monoclonal Antibodies ,
J Chromatogr A
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Arnon, R. and Neurath, H.
An Immunological Approach to the Study of Evolution of Trypsins ,
Proc Natl Acad Sci U S A
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Ascenzi, P. , Amiconi, G. , Bolognesi, M. , Menegatti, E. and Guarneri, M.
Trypsin Activation. Effect of the Ile-Val Dipeptide Concentration on Kazal Inhibitor Binding to Bovine Trypsinogen ,
Biochim Biophys Acta
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Ascenzi, P. , Bolognesi, M. , Guarneri, M. , Menegatti, E. and Amiconi, G.
Benzamidine as a Spectroscopic Probe for the Primary Specificity Subsite of Trypsin-like Proteinases ,
Mol Cell Biochem
 64 , 139 , 1984
Ascenzi, P. , Menegatti, E. , Bortolotti, F. , Guarneri, M. and Antonini, E.
Steady-state and Pre-steady-state Kinetics of the Trypsin-catalyzed Hydrolysis of a-CBZ-L-Lysine-p-nitrophenyl Ester ,
Biochim Biophys Acta
 658 , 158 , 1981
Asgeirsson, B. , Fox, J. and Bjarnason, J.
Purification and Characterization of Trypsin from the Poikilotherm Gladus morhua ,
Eur J Biochem
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Ashton, D. , Ashcroft, A. , Beddell, C. , Green, B. and Oliver, R.
On the Analysis of Bovine Trypsin by Electrospray-Mass Spectrometry ,
Biochem Biophys Res Commun
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Atassi, P.
Surface-simulation Synthesis of the Substrate-binding Site of an Enzyme. Demonstration with Trypsin ,
Biochem J
 226 , 477 , 1985
Baines, N. , Baird, J. and Elmore, D.
The Kinetics of Hydrolysis of Derivatives of Arginine, Homoarginine and Ornithine by Trypsin ,
Biochem J
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Balls, A.
Concerning Trypsinogen ,
Proc Natl Acad Sci U S A
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Banumathi, E. , Haribalaganesh, R. , Babu, S. , Kumar, N. and Sangiliyandi, G.
High-yielding Enzymatic Method for Isolation and Culture of Microvascular Endothelial Cells from Bovine Retinal Blood Vessels ,
Microvasc Res
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Bar-Eli, A. and Katchalski, E.
A Water-Insoluble Trypsin Derivative and its Use as a Trypsin Column ,
Nature
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Bartholomew, J. , Handley, C. and Lowther, D.
The Effects of Trypsin Treatment on Proteoglycan Biosynthesis of Bovine Articular Cartilage ,
Biochem J
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Beardslee, R. and Zahnley, J.
A Simple Preparation of beta-Trypsin Based on a Colorimetric Study of the Thermal Stabilities of alpha and beta Trypsin ,
Arch Biochem Biophys
 158 , 806 , 1973
Berezin, I. , Kazanskaya, N. , Klyosov, A. and Svedas, V.
The Mechanism of the alpha-Chymotrypsin and Trypsin-Catalyzed Hydrolysis of Amides. Evidence for the Participation of the Active Serine in the Amidase Activity of Trypsin ,
Eur J Biochem
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Bergmann, M. and Fruton, J.
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Berlin, I. and Neujahr, H.
Studies of Controlled Lysis of Washed Cell Suspensions of Lactobacillus fermenti and Preparation of Membrane-like Fragments by a Combined Trypsin-Lysozyme Treatment ,
Acta Chem Scand
 22 , 2972 , 1968
Berliner, L. and Wong, S.
Evidence Against Two "pH-locked" Conformations of Phosphorylated Trypsin ,
J Biol Chem
 248 , 1118 , 1973
Bier, M. and Nord, F.
On the Mechanism of Enzyme Action. 46. The Effect of Certain Ions on Crystalline Trypsin and Reinvestigation of its Isoelectric Point ,
Arch Biochem Biophys
 33 , 320 , 1951
Bricteux-Gregoire, S. , Schyns, R. and Florkin, M.
N-Terminal Amino Acid Sequence of Trypsinogen from the Elephant Seal Mirounga leonine L. (Carnivora) ,
Biochim Biophys Acta
 351 , 87 , 1974
Brines, R. and Brock, J.
The Effect of Trypsin and Chymotrypsin on the in Vitro Antimicrobial and Iron-Binding Properties of Lactoferrin in Human Milk and Bovine Colostrum ,
Biochim Biophys Acta
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Brunger, A. , Huber, R. and Karplus, M.
Trypsinogen-Trypsin Transition: A Molecular Dynamics Study of Induced Conformational Change in the Activation Domain ,
Biochemistry
 26 , 5153 , 1987
Byrne, R. and Scanu, A.
Soluble and Immobilized Trypsins as Structural Probes of Human Plasma High-Density Lipoproteins: Enzyme Properties and Kinetics of Proteolysis ,
Biochemistry
 22 , 2894 , 1983
Caldwell, R.
Effect of Calcium and Phytic Acid on the Activation of Trypsinogen and the Stability of Trypsin ,
J Agric Food Chem
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Castaneda-Agullo, M. and Del Castillo, L.
The Influence of the Medium Dielectric Strength upon Trypsin Kinetics ,
J Gen Physiol
 42 , 617 , 1959
Chambers, J. , Christoph, G. , Krieger, M. , Kay, L. and Stroud, R.
Silver Ion Inhibition of Serine Proteases. Crystallographic Study of Silver-Trypsin ,
Biochem Biophys Res Commun
 59 , 70 , 1974
Chang, A. and Slayman, C.
A Structural Change in the Neurospora Plasma Membrane [H+] ATPase Induced by N-Ethylmaleimide ,
J Biol Chem
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Chen, N. , Zou, J. , Wang, S. , Ye, Y. , Huang, Y. , Gadda, G. and Yang, J.
Designing Protease Sensors for Real-time Imaging of Trypsin Activation in Pancreatic Cancer Cells ,
Biochemistry
 48 , 3519 , 2009
Chen, T. and Reisler, E.
Tryptic Digestion of Rabbit Skeletal Myofibrils: An Enzymatic Probe of Myosin Cross-Bridges ,
Biochemistry
 23 , 2400 , 1984
Christensen, U. and Sottrup-Jensen, L.
Mechanism of alpha-2-Macroglobulin - Proteinase Interaction. Studies with Trypsin and Plasmin ,
Biochemistry
 23 , 6619 , 1984
Coats, E.
Comparative Inhibition of Thrombin, Plasmin, Trypsin, and Complement by Benzamidines Using Substituent Constants and Regression Analysis ,
J Med Chem
 16 , 1102 , 1973
Cohen, W. , Lache, M. and Erlanger, B.
The Reactivation of Diethylphosphoryltrypsin ,
Biochemistry
 1 , 686 , 1962
Coletta, M. , Ascenzi, P. , Amiconi, G. , Bolognesi, M. , Guarneri, M. and Menegatti, E.
Bovine Trypsinogen Activation. A Thermodynamic Study ,
Biophys Chem
 37 , 355 , 1990
Compton, P. and Fink, A.
Low-Temperature Reaction of Trypsin with p-Nitroanilide Substrates. Tetrahedral Intermediate Formation on Enzyme Isomerization ,
Biochemistry
 23 , 2989 , 1984
Conners, R. , Konarev, A. , Forsyth, J. , Lovegrove, A. , Marsh, J. , Joseph-Horne, T. , Shewry, P. and Brady, R.
An Unusual Helix-turn-helix Protease Inhibitory Motif in a Novel Trypsin Inhibitor from Seeds of Veronica ,
J Biol Chem
 282 , 27760 , 2007
Craik, C. , Roczniak, S. , Largman, C. and Rutter, W.
The Catalytic Role of the Active Site Aspartic Acid in Serine Proteases ,
Science
 237 , 909 , 1987
Cunningham, L.
Molecular-Kinetic Properties of Crystalline Diisopropyl Phosphoryl Trypsin ,
J Biol Chem
 211 , 13 , 1954
D'Angelo, M. , Visintin, J. , Richtzenhain, L. and Goncalves, R.
Evaluation of Trypsin Treatment on the Inactivation of Bovine Herpesvirus Type 1 on In Vitro Produced Pre-implantation Embryos ,
Reprod Dom Anim
 44 , 536 , 2008
Delaage, M. and Lazdunski, M.
Different Molecular Species of Bovine Trypsinogen and Trypsin (French) ,
Biochim Biophys Acta
 105 , 608 , 1965
DelCastillo, L. , Davila, G. , Dorantes, L. , Oliver, C. , Ibarra, R. and Castaneda-Agullo, M.
The Influence of a Free alpha-Ammonium Group in the Substrate Upon Trypsin-catalyzed Transesterification ,
Biochim Biophys Acta
 191 , 354 , 1969
Delvaux, A. , Vanderelst, L. and Octave, J.
Inhibition of Trypsin by the beta-Amyloid Protein Precursor - A Comparative Study Between Transfected Cells, Human Brain and Cerbrospinal Fluid ,
F.E.B.S. Lett.
 297 , 124 , 1992
Desnuelle, P.
Trypsin , The Enzymes Vol. 4 , P. Boyer, H. Lardy, and K. Myrback , Academic Press, NY , 119 , 1960
Dominko, T. , Ramalho-Santos, J. , Chan, A. , Moreno, R. , Luetjens, C. , Simerly, C. , Hewitson, L. , Takahashi, D. , Martinovich, C. , White, J. and Schatten, G.
Optimization Strategies for Production of Mammalian Embryos by Nuclear Transfer ,
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Erlanager, B. , Kokowsky, N. and Cohen, W.
The Preparation and Properties of Two New Chromogenic Substrates of Trypsin ,
Arch Biochem Biophys
 95 , 271 , 1961
Feinstein, G.
Purification of Trypsin by Affinity Chromatography on Ovomucoid-sepharose Resin ,
F.E.B.S. Lett.
 7 , 353 , 1970
Figarella, C. , Negri, G. and Guy, O.
The Two Human Trypsinogens. Inhibition Spectra of the Two Human Trypsins Derived from Their Purified Zymogens ,
Eur J Biochem
 53 , 457 , 1975
Finer-Moore, J. , Kossiakoff, A. , Hurley, J. , Earnest, T. and Stroud, R.
Solvent Structure in Crystals of Trypsin Determined by X-Ray and Neutron Diffraction ,
Proteins, Structure Function & Genetics
 12 , 203 , 1992
Finotti, P.
Separation by Heparin-affinity Chromatography of Catalytically Active and Inactive Forms of Trypsin which Retain the (Na-K)ATPase Stimulating Property ,
Clin Chim Acta
 256 , 37 , 1996
Ford, J. , Chambers, R. and Cohen, W.
An Active-site Titration Method for Immobilized Trypsin ,
Biochim Biophys Acta
 309 , 175 , 1973
Fraenkel-Conrat, H. , Bean, R. and Lineweaver, H.
Essential Groups for the Interaction of Ovomucoid (Egg White Trypsin Inhibitor) and Trypsin, and for Tryptic Activity ,
J Biol Chem
 177 , 385 , 1949
Fromherz, P. and Marcheva, D.
Enzyme Kinetics at a Lipid Protein Monolayer. Induced Substrate Inhibition of Trypsin ,
F.E.B.S. Lett.
 49 , 329 , 1975
Fujioka,T. , Tanizawa, K. and Kanaoka, Y.
Specific Spin-Labelling at Trypsin Active Site. Application of "Inverse Substrate" to the Structural Analysis of the Active Site ,
Biochim Biophys Acta
 612 , 205 , 1980
Gabel, D. , Vretblad, P. , Axen, R. and Porath, J.
Insolubilized Trypsin with Activity in 8 M Urea ,
Biochim Biophys Acta
 214 , 561 , 1970
Gavilanes-Ruiz, M. , Tommasino, M. and Capaldi, R.
Structure-Function Relationships of the Escherichia coli ATP Synthase Probed by Trypsin Digestion ,
Biochemistry
 27 , 603 , 1988
Gendry, P. and Launay, J.
Pancreatic Anionic Trypsin - Evidence for the Existence of a 30-kDa Form ,
Comp Biochem Physiol B
 102 , 37 , 1992
Ghiron, C. , Longworth, J. and Ramachandran, J.
Triplet-Triplet Energy Transfer in alpha-Trypsin ,
Proc Natl Acad Sci U S A
 70 , 3703 , 1973
Glenner, G. , Hopsu, V. and Cohen, L.
New Substrates of Trypsin and Some Trypsin-like Enzymes ,
J Histochem Cytochem
 12 , 545 , 1964
Gomez, J. , Birnbaum, E. and Darnall, D.
The Metal Ion Acceleration of the Conversion of Trypsinogen to Trypsin. Lanthanide Ions as Calcium Ion Substitutes ,
Biochemistry
 13 , 3745 , 1974
Graf, L. , Hegyi, G. , Liko, I. , Hep, J. , Medzihradszky, K. , Craik, C. and Rutter, W.
Structural and Functional Integrity of Specificity and Catalytic Sites of Trypsin ,
Int J Pept Protein Res
 32 , 512 , 1988
Graf, L. , Craik, C. , Patthy, A. , Roczniak, S. , Fletterick, R. and Rutter, W.
Selective Alteration of Substrate Specificity by Replacement of Aspartic Acid-189 with Lysine in the Binding Pocket of Trypsin ,
Biochemistry
 26 , 2616 , 1987
Green, M. , Gladner, J. , Cunningham, L. and Neurath, H.
The Effects of Divalent Cations on the Enzymatic Activities of Trypsin and alpha-Chymotrypsin ,
J Am Chem Soc
 74 , 2122 , 1952
Green, S. and Neurath, H.
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Greenbaum, L. , Hirshkowitz, A. and Schoichet, I.
The Activation of Trypsinogen by Cathepsin B ,
J Biol Chem
 234 , 2885 , 1959
Griffiths, A. and Brechner, A.
Protection Afforded to Trypsin and Trypsinogen by Calcium Ion from Inactivation by Chlorambucil ,
Proc Soc Exp Biol Med
 142 , 1045 , 1973
Hartley, B.
Homologies in Serine Proteinases ,
Phil Trans R Soc Lond
 257 , 77 , 1970
Helmqvist, B. , Borgstrs<caron>m, A. and Ohlsson, K.
Interactions in Vitro and in vivo Between Anionic and Cationic Porcine Trypsin and Porcine Plasma Proteinase Inhibitors ,
Biol Chem Hoppe Seyler
 369 , 1331 , 1988
Hermodson, M. , Ericsson, L. , Neurath, H. and Walsh, K.
Determination of the Amino Acid Sequence of Porcine Trypsin by Sequenator Analysis ,
Biochemistry
 12 , 3146 , 1973
Hess, G. and Wainfan, E.
Enzymatically Active Components in Trypsin Autolysates ,
J Am Chem Soc
 80 , 501 , 1958
Higaki, J. and Light, A.
Independent Refolding of Domains in the Pancreatic Serine Proteinases ,
J Biol Chem
 261 , 10606 , 1986
Hixson, H. and Nishikawa, A.
Affinity Chromatography: Purification of Bovine Trypsin and Thrombin ,
Arch Biochem Biophys
 154 , 501 , 1973
Hofmann, T.
The Purification and Properties of Fragments of Trypsinogen Obtained by Cyanogen Bromide Cleavage ,
Biochemistry
 3 , 356 , 1964
Holeysovsky, V. , Keil, B. and Sorm, F.
Location of Reactive Tyrosine Residues in Trypsin ,
F.E.B.S. Lett.
 3 , 107 , 1969
Houston, L. and Walsh, K.
The Transient Inactivation of Trypsin by Mild Acetylation with N-Acetylimidazole ,
Biochemistry
 9 , 156 , 1970
Ikeno, K. , Ikeno, T. , Kazuya, H. and Ishiguro, I.
Purification and Characterization of a Trypsin-like Protease in the Submandibular Gland of Rats ,
J. Biochem.
 99 , 1219 , 1986
Isackson, P. , Beaudoin, J. , Hermodson, M. and Reeck, G.
Production of HMG-3 by Limited Trypsin Digestion of Purified High-Mobility-Group Nonhistone Chromatin Proteins ,
Biochim Biophys Acta
 748 , 436 , 1983
Iwaki, K. , Ogawa, M. , Kitahara, T. , Tanaka, S. and Kosaki, G.
Influence of Inactivation of Trypsin on Immunoreactivity and Serum Immunoreactive Trypsin Concentration Measured by Radioimmunoassay ,
Enzyme
 29 , 153 , 1983
Jameson, G. and Elmore, D.
Affinity Chromatography of Bovine Trypsin. A Rapid Separation of Bovine alpha and beta Trypsin ,
Biochem J
 141 , 555 , 1974
Jeno, P. , Green, J. and Lentze, M.
Specificity Studies on Enteropeptidase Substrates Related to the N-Terminus of Trypsinogen ,
Biochem J
 241 , 721 , 1987
Jones, R.
Unusual Fucoidin-Binding Properties of Chymotrypsinogen and Trypsinogen ,
Biochim Biophys Acta
 1037 , 227 , 1990
Jurasek, L. and Smillie, L.
The Amino Acid Sequence of Streptomyces griseus Trypsin II. The Tryptic Peptides ,
Can J Biochem
 52 , 382 , 1974
Kasai, K. and Ishii, S.
Unimportance of Histidine and Serine Residues of Trypsin in the Substrate Binding Function Proved by Affinity Chromatography ,
J. Biochem.
 74 , 631 , 1973
Kawasaki, H. , Kurosu, Y. , Kasai, H. , Isobe, T. and Okuyama, T.
Limited Digestion of Calmodulin with Trypsin in the Presence or Absence of Various Metal Ions ,
J. Biochem.
 99 , 1409 , 1986
Kay, C. , Smillie, L. and Hilderman, F.
The Molecular Weight of Trypsinogen ,
J Biol Chem
 236 , 118 , 1961
Keil -Dlouha, V. and Keil, B.
A Tryptophan Residue in Bovine Trypsinogen Essential for its Potential Enzymic Activity and for its Interaction with Basic Pancreatic Trypsin Inhibitor ,
J Mol Biol
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Keil-Dlouha, V. , Zylber, N. , Imhoff, J. , Tong, N. and Keil, B.
Proteolytic Activity of Pseudotrypsin ,
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 16 , 291 , 1971
Keil-Dlouha, V. , Zylber, N. , Tong, N. and Keil, B.
Cleavage of Glucagon by alpha- and beta-Trypsin ,
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 16 , 287 , 1971
Knights, R. and Light, A.
Sepharose-Bound Trypsin and Activated Sepharose-Bound Trypsinogen. Studies with Small and Large Substrates ,
Arch Biochem Biophys
 160 , 377 , 1974
Knights, R. and Light, A.
Enhanced Reactivity of Disulfide-Modified Trypsinogen Toward an Active-Site Directed Reagent ,
Biochem Biophys Res Commun
 61 , 1161 , 1974
Kobayashi, R. and Ishii, S.
The Trypsin-catalyzed Hydrolysis of Some L-alpha-amino-lacking Substrates ,
J. Biochem.
 75 , 825 , 1974
Konishi, K. and Takagi, T.
Activation of the Fibrin Stabilizing Factor by Trypsin and Some of Its Properties After Activation ,
J. Biochem.
 65 , 281 , 1969
Kossiakoff, A. , Chambers, J. , Kay, L. and Stroud, R.
Structure of Bovine Trypsinogen at 1.9 Å Resolution ,
Biochemistry
 16 , 654 , 1977
Kossiakoff, A.
Protein Dynamics Investigated by the Neutron Diffraction-Hydrogen Exchange Technique ,
Nature
 296 , 713 , 1982
Kossiakoff, A.
Tertiary Structure Is a Principal Determinant to Protein Deamidation ,
Science
 240 , 191 , 1988
Koutsopoulos, S. , Patzsch, K. , Bosker, W. and Norde, W.
Adsorption of Trypsin on Hydrophilic and Hydrophobic Surfaces ,
Langmuir
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Krebs, G. and Jacquot-Armond, Y.
Interactions between Trypsin, alpha-2 Macroglobulin and Soybean Trypsin Inhibitor ,
Biochem Biophys Res Commun
 55 , 929 , 1973
Kubiak, T. and Cowburn, D.
Trypsin-Catalyzed Formation of Pig Des-(23-63)-Proinsulin from Desoctapeptide-(B23-30)-insulin ,
Biochem J
 234 , 665 , 1986
Kunitz, M. and Northrop, J.
Isolation from Beef Pancreas of Crystalline Trypsinogen, Trypsin, a Trypsin Inhibitor and an Inhibitor-Trypsin Compound ,
J Gen Physiol
 19 , 991 , 1936
Kunugi, S. , Fukuda, M. and Ise, N.
Pressure Dependence of Trypsin-Catalyzed Hydrolyses of Specific Substrates ,
Biochim Biophys Acta
 704 , 107 , 1982
Leef, J. and Larner, J.
Insulin-mimetic Effect of Trypsin on the Insulin Receptor Tyrosine Kinase in Intact Adipocytes ,
J Biol Chem
 262 , 14837 , 1987
Liem, R. and Scheraga, H.
Mechanism of Action of Thrombin or Fibrinogen. IV. Further Mapping on the Active Sites of Thrombin and Trypsin ,
Arch Biochem Biophys
 160 , 333 , 1974
Liener, I.
Chromatographic Studies on Trypsin, Trypsinogen and the Activation Process ,
Arch Biochem Biophys
 88 , 216 , 1960
Liepinsh, E. and Otting, G.
Specificity of Urea Binding to Proteins ,
J Am Chem Soc
 116 , 9670 , 1994
Light, A. and Odorzynski, T.
Refolding of Bovine Trypsinogen with One and Two Disulfide Bonds Reduced and Carboxymethylated ,
J Biol Chem
 254 , 9162 , 1979
Light, A. and Fonseca, P.
The Preparation and Properties of the Catalytic Subunit of Bovine Enterokinase ,
J Biol Chem
 259 , 13195 , 1984
Lindley, H.
A New Synthetic Substrate for Trypsin and Its Application to the Determination of the Amino-acid Sequence of Proteins ,
Nature
 178 , 647 , 1956
Liu, K. , Markakis, P. and Smith, D
Trypsin Inhibition by Free Fatty Acids and Stearoyl-CoA ,
J Agric Food Chem
 38 , 1475 , 1990
Luong, J. , Male, K. and Nguyen, A.
A Continuous Affinity Ultrafiltration Process for Trypsin Purification ,
Biotechnol Bioeng
 31 , 516 , 1988
Luong, J. , Male, K. and Nguyen, A.
Synthesis and Characterization of a Water-Soluble Affinity Polymer for Trypsin Purification ,
Biotechnol Bioeng
 31 , 439 , 1988
MacKenzie, N. , Malthouse, J. and Scott, A.
Cryoenzymology of Trypsin. 13C-NMR Detection of an Acyl-trypsin Intermediate in the Trypsin-Catalyzed Hydrolysis of a Highly Specific Substrate at Subzero Temperature ,
Biochem J
 219 , 437 , 1984
Mallory, P. and Travis, J.
Human Pancreatic Enzymes. Characterization of Anionic Human Trypsin ,
Biochemistry
 12 , 2847 , 1973
Mannhalter, C. , Schiffman, S. and Jacobs, A.
Trypsin Activation of Human Factor XI ,
J Biol Chem
 255 , 2667 , 1980
Mares-Guia, M. and Figueiredo, A.
Thermodynamics of the Hydrophobic Interaction in the Active Center of Trypsin. Investigation with Amidines and Guanidines ,
Biochemistry
 9 , 3223 , 1970
Mares-Guia, M. and Shaw, E.
Studies on the Active Center of Trypsin. The Binding of Amidines and Guanidines as Models of the Substrate Side Chain ,
J Biol Chem
 240 , 1579 , 1965
Mares-Guia, M. , Silva, E. and Tunes, H.
Competitive Inhibition of the D-Isomer in Racemic Mixtures Used as Substrate in Kinetic Studies: A Simple Method for Data Treatment ,
Arch Biochem Biophys
 228 , 278 , 1984
Markwardt, F. , Richter, M. , Walsmann, P. and Landmann, H.
The Inhibition of Trypsin, Plasmin, and Thrombin by Benzyl - 4 - Guanidinobenzoate and 4' - Nitrobenzyl 4 - Guanidinobenzoate ,
F.E.B.S. Lett.
 8 , 170 , 1970
Maroux, S. , Rovery, M. and Desnuelle, P.
Hydrolysis by Bovine Trypsin of Some Aromatic Bonds in High Molecular Weight Peptides ,
Biochim Biophys Acta
 122 , 147 , 1966
Martinek, K. , Goldmacher, V. , Klibanov, A. and Berezin, I.
Denaturing Agents (Urea and Acrylamide) Protect Enzymes Against Irreversible Thermoinactivators: A Study with Native and Immobilized alpha-Chymotrypsin and Trypsin ,
F.E.B.S. Lett.
 51 , 152 , 1975
Matsushima, A.
States of Amino Acid Residues in Proteins. XVII. Tyrosine, Histidine and Tryptophan Residues in Bovine Trypsin in the Presence and Absence of Benzamidine ,
J. Biochem.
 65 , 961 , 1969
Maurel, P. , Hoa, G. and Douzon, P.
The pH Dependence of the Tryptic Hydrolysis of Benzoyl-L-arginine Ethyl Ester in Cooled Mixed Solvents ,
J Biol Chem
 250 , 1376 , 1975
Mayer, M. , Khassis, S. and Shafrir, E.
Determination of Trypsin by Its Accelerating Effect on the Onset of Trypsinogen Activation ,
Anal Biochem
 58 , 25 , 1974
McMurray, J. and Dyckes, D.
Evidence for Hemiketals as Intermediates in the Inactivation of Serine Proteinases with Halomethyl Ketones ,
Biochemistry
 25 , 2298 , 1986
Menegatti, E. , Guarneri, M. , Bolognesi, M. , Ascenzi, P. and Amiconi, G.
Activating Effect of the Ile-Val Dipeptide on the Catalytic Properties of Bovine Trypsinogen ,
Biochim Biophys Acta
 832 , 1 , 1985
Mitin, Y. , Zapevalova, N. and Gorbunova, E.
New Approaches to Peptide Synthesis with the Help of Trypsin ,
Biomed Biochim Acta
 50 , S74 , 1991
Mohan, S. , Jennings, J. , Linkhart, T. and Baylink, D.
Primary Structure of Human Skeletal Growth Factor: Homology with Human Insulin-like Growth Factor-II ,
Biochim Biophys Acta
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Inactivation of Trypsinogen by Methane Sulfonyl Fluoride ,
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 41 , 108 , 1974
Moroi, M. and Yamasaki, M.
Mechanism of Interaction of Bovine Trypsin with Human alpha-1-Antitrypsin ,
Biochim Biophys Acta
 359 , 130 , 1974
Muller, O. and Yamanouchi, I.
Stable Solutions of Trypsin ,
Arch Biochem Biophys
 76 , 328 , 1958
Muramatu, M. and Fujii, S.
Inhibitory Effects of omega-Amino Acid Esters on the Activities of Trypsin, Plasmin, and Thrombin ,
J. Biochem.
 65 , 17 , 1969
Murray, P. , Silberstein, S. , Cantore, M. and Passeron, S.
A Radioactive Method for the Measurement of Trypsin and Trypsin-like Activities ,
Anal Biochem
 179 , 56 , 1989
Neurath, H.
The Activation of Zymogens ,
Adv Protein Chem
 12 , 319 , 1957
Neurath, H. and Schwert, G.
Crystalline Proteolytic Enzymes ,
Chem Rev
 46 , 69 , 1950
Nishino, N. , Mitsuyasu, N. and Izumiya, N.
Action of Trypsin on Synthetic Substrates. IV. Hydrolyses of Synthetic Insulin Fragments by Trypsin ,
J. Biochem.
 75 , 979 , 1974
Nord, F. and Bier, M.
On the Mechanism of Enzyme Action. LV. A Study of the Interaction between Calcium and Trypsin ,
Biochim Biophys Acta
 12 , 56 , 1953
Nord, F. , Bier, M. and Terminiello, L.
On the Mechanism of Action. LXI. The Self Digestion of Trypsin, Calcium-Trypsin and Acetyltrypsin ,
Arch Biochem Biophys
 65 , 120 , 1956
Northrop, J. and Kunitz, M.
Crystalline Trypsin. I. Isolation and Tests of Purity ,
J Gen Physiol
 16 , 267 , 1932
Northrop, J. , Kunitz, M. and Herriott, R.
, Crystalline Enzymes , Columbia Univ Press , 125 , 1948
Nureddin, A. and Ingami, T.
Chemical Modification of Amino Groups and Guanidino Groups of Trypsin. Preparation of Stable and Soluble Derivatives ,
Biochem J
 147 , 71 , 1975
Odorzynski,T. and Light, A.
Refolding of the Mixed Disulfide of Bovine Trypsinogen and Glutathione ,
J Biol Chem
 254 , 4291 , 1979
Ohlsson, K. and Tegner, H.
Anionic and Cationic Dog Trypsin. Isolation and Partial Characterization ,
Biochim Biophys Acta
 312 , 328 , 1973
Ohshima, Y. , Suzuki, Y. , Nakatani, A. and Nohara, D.
Refolding of Fully Reduced Bovine Pancreatic Trypsin ,
J Biosci Bioeng
 106 , 345 , 2008
Olafson, R. and Smillie, L.
Enzymic and Physicochemical Properties of Streptomyces griseus Trypsin ,
Biochemistry
 14 , 1161 , 1975
Olafson, R. , Jurasek, L. , Carpenter, M. and Smillie, L.
Amino Acid Sequence of Streptomyces griseus Trypsin. Cyanogen Bromide Fragments and Complete Sequence ,
Biochemistry
 14 , 1168 , 1975
Ooms, A. and van Dijk, C.
The Reaction of Organophosphorus Compounds with Hydrolytic Enzymes - III. The Inhibition of Chymotrypsin and Trypsin ,
Biochem Pharmacol
 15 , 1361 , 1966
Pace, C. and Barrett, A.
Kinetics of Tryptic Hydrolysis of the Arginine-Valine Bond of Folded and Unfolded Ribonuclease T1 ,
Biochem J
 219 , 411 , 1984
Perkal, M. , Marks, C. , Lorber, M. and Marks, W.
A Three-Year Experience with Serum Anodal Trypsinogen as a Biochemical Marker for Rejection in Pancreatic Allografts - False Postives, Tissue Biopsy, Comparison with Other Markers, and Diagnostic Strategies ,
Transplantation
 53 , 415 , 1992
Perlmutter, D. , Joslin, G. , Nelson, P. , Schasteen, C. , Adams, S. and Fallon, R.
Endocytosis and Degradation of alpha-1-Antitrypsin-Protease Complexes Is Mediated by the Serpin-Enzyme Complex (SEC) Receptor ,
J Biol Chem
 265 , 16713 , 1990
Pitotti, A. , Maurich, V. , Moneghini, M. , Franchi, G. and Lencioni, E.
A Sensitive High-Performance Liquid Chromatographic Assay for Trypsin-Like Enzymes ,
J Pharm Biomed Anal
 6 , 121 , 1988
Polanowski, A. , Cieslar, E. , Otlewski, J. , Nienartowicz, B.,Wilimowska-Pelc, A. and Wilusz, T.,
Protein Inhibitors of Trypsin from the Seeds of Cucurbitaceae Plants ,
Acta Biochim Pol
 34 , 395 , 1987
Poncz, L. and Dearborn, D.
The Resistance to Tryptic Hydrolysis of Peptide Bonds Adjacent to N-epsilon, N-Dimethyllysyl Residues ,
J Biol Chem
 258 , 1844 , 1983
Porter, W. and Preston, J.
Retention of Trypsin and Chymotrypsin Proteolytic Activity in Sodium Dodecyl Sulfate Solutions ,
Anal Biochem
 66 , 69 , 1975
Ram, J. , Terminiello, L. , Bier, M. and Nord, F.
On the Mechanism of Enzyme Action. LVIII. Acetyltrypsin, A Stable Trypsin Derivative ,
Arch Biochem Biophys
 52 , 464 , 1954
Rayasduarte, P. , Bergeron, D. and Nielsen, S.
Screening of Heat-Stable Trypsin Inhibitors in Dry Beans and Their Partial Purification from Great Northern Beans (Phaseolus-Vulgaris) Using Anhydrotrypsin Sepharose Affinity Chromatography ,
J Agric Food Chem
 40 , 32 , 1992
Read, R. , Brayer, G. , Jurasek, L. and James, M.
Critical Evaluation of Comparative Model Building of Streptomyces griseus Trypsin ,
Biochemistry
 23 , 6570 , 1984
Reeck, G. and Neurath, H.
Pancreatic Trypsinogen from the African Lungfish ,
Biochemistry
 11 , 503 , 1972
Reichart, E. , Boerkmann, P. , Vignaud, J. and Plenat, F.
Experimental Emphysema Following One Intravenous Infusion of Trypsin ,
Exp Lung Res
 18 , 45 , 1992
Rice, R. , Means, G. and Brown, W.
Stabilization of Bovine Trypsin by Reductive Methylation. ,
Biochim Biophys Acta
 492 , 316-21 , 1977
Ridderknecht, H. , Fleming, R. and Geokus, M.
Effect of alpha-2 Macroglobulin on Some Kinetic Parameters of Trypsin ,
Biochim Biophys Acta
 377 , 158 , 1975
Riechmann, L. and Kasche, V.
Kinetic Studies on the Mechanism and the Specificity of Peptide Semisynthesis Catalyzed by the Serine Proteases alpha-Chymotrypsin and beta-Trypsin ,
Biochem Biophys Res Commun
 120 , 686 , 1984
Robinson, N. , Neurath, H. and Walsh, K.
Preparation and Characterization of Guanidated Trypsinogen and E-Guanidinated Trypsin ,
Biochemistry
 12 , 414 , 1973
Robinson, N. , Neurath, H. and Walsh, K.
The Relation of the alpha-Amino Group of Trypsin to Enzyme Function and Zymogen Activation ,
Biochemistry
 12 , 420 , 1973
Royer, G. and Uy, R.
Evidence for the Induction of a Conformational Change of Bovine Trypsin by a Specific Substrate at pH 8.0 ,
J Biol Chem
 248 , 2627 , 1973
Ryltsev, V. and Virnik, R.
Kinetic Study on Isolation of Trypsin Immobilized on Dialdehyde Cellulose During Hydrolytic Destruction ,
Antibiot Chemother
 34 , 202 , 1989
Sarkany, R. and Moreland, B.
Enhancement of the Autocatalytic Activation of Trypsinogen to Trypsin by Bile and Bile Acids ,
Biochim Biophys Acta
 839 , 262 , 1985
Sattar, S. , Abbas, B. , Jones, L. , Saridogan, E. , Mahmood, T. , Mehta, J. and Djahanbakhch, O.
Comparison of the Growth Patterns and Morphological Characteristics of Mechanically and Enzymatically Isolated Fallopian Tube Epithelial Cells ,
Cell Biol Int
 23 , 379 , 1999
Sawada, H. , Kawahigashi, M. , Yokosawa, H. and Ishii, S.
Trypsin-like Enzyme from Eggs of the Ascidian (Protochordate) Halocnthia roretzi ,
J Biol Chem
 260 , 15694 , 1985
Schaffer, N. , Engle, R. , Simet, L. , Drisko, D. and Harshman, S.
Phosphopeptides from Chymotrypsin and Trypsin after Inactivation of P32 Labeled DFP and Sarin ,
Fed Proc
 15 , 347 , 1956
Schilling, R. and Mitra, A.
Degradation of Insulin by Trypsin and Alpha-Chymotrypsin ,
Pharm Res
 8 , 721 , 1991
Schroeder, D. and Shaw, E.
Chromatography of Trypsin and Its Derivatives. Characterization of a New Active Form of Bovine Trypsin ,
J Biol Chem
 243 , 2943 , 1968
Schuchert-Shi Aiping, Hauser PeterC.
Peptic and tryptic digestion of peptides and proteins monitored by capillary electrophoresis with contactless conductivity detection. ,
Anal Biochem
 387 , 202-7 , 2009
Shaw, E. and Glover, G.
Further Observations on Substrate-Derived Chloromethyl Ketones that Inactivate Trypsin ,
Arch Biochem Biophys
 139 , 298 , 1970
Shtelzer, S. , Rappoport, S. , Avnir, D. , Ottolenghi, M. and Braun, S.
Properties of Trypsin and of Acid Phosphatase Immobilized in Sol-Gel Glass Matrices ,
Biotechnol Appl Biochem
 15 , 227 , 1992
Sipos, T. and Merkel, J.
An Effect of Calcium Ions on the Activity, Heat Stability, and Structure of Trypsin ,
Biochemistry
 9 , 2766 , 1970
Smillie, L. and Kay, C.
Abnormal Tyrosine Ionization and Configurational Changes of Trypsinogen in Alkaline Solutions ,
J Biol Chem
 236 , 112 , 1961
Smillie, L. and Neurath, H.
Reversible Inactivation of Trypsin by Anhydrous Formic Acid ,
J Biol Chem
 234 , 355 , 1959
Smith, R. and Shaw, E.
Pseudotrypsin. A Modified Bovine Trypsin Produced by Limited Autodigestion ,
J Biol Chem
 244 , 4704 , 1969
Soleimani, M. and Nadri, S.
A Protocol for Isolation and Culture of Mesenchymal Stem Cells from Mouse Bone Marrow ,
Nat Protoc
 4 , 102 , 2009
Stevenson, K. and Voordouw, J.
Characterization of Trypsin and Elastase from the Moose (Alces alces). I. Amino Acid Composition and Specificity Towards Polypeptides ,
Biochim Biophys Acta
 386 , 324 , 1975
Stewart, J. , Lee, H. and Dobson, J.
Evidence for a Functional Carboxyl Group in Trypsin and Chymotrypsin ,
J Am Chem Soc
 85 , 1537 , 1963
Stewart, K.
A Method for Automated Analyses of the Activities of Trypsin, Chymotrypsin and Their Inhibitors ,
Anal Biochem
 51 , 11 , 1973
Stroud, R. , Kay, L. and Dickerson, R.
The Structure of Bovine Trypsin: Electron Density Maps of the Inhibited Enzyme at 5 Å and at 27 Å Resolution ,
J Mol Biol
 83 , 185 , 1974
Sturzebecher, J.
Stable Acyl-Derivatives of Trypsin-like Enzymes. Preparation, Kinetics, Application ,
Biomed Biochim Acta
 45 , 1405 , 1986
Tallan, H.
Chromatography of Trypsinogen ,
Biochim Biophys Acta
 27 , 407 , 1958
Tanaka, T. , McRae, B. , Cho, K. , Cook, R. , Fraki, J. , Johnson, D. and Powers, J.
Mammalian Tissue Trypsin-like Enzymes. Comparative Reactivities of Human Skin Tryptase, Human Lung Tryptase, and Bovine Trypsin with Peptide 4-nitroanilide and Thioester Substrates ,
J Biol Chem
 258 , 13552 , 1983
Taran, L. and Smovdyr, I.
Comparative Kinetic Investigations of the Primary Specificity of Bovine and Salmon Trypsins. Russian ,
Biochem Z
 57 , 39 , 1992
Terminiello, L. , Ram, S. , Bier, M. and Nord, F.
On the Mechanism of Enzyme Action. LX. Acyl Derivatives of Trypsin ,
Arch Biochem Biophys
 57 , 252 , 1955
Tietze, F.
Molecular-Kinetic Properties of Crystalline Trypsinogen ,
J Biol Chem
 204 , 1 , 1953
Tisljar, U. and Denker, W.
A Sensitive Assay for Proteolytic Activity Using Fluorescein-Labeled Gelatin Coupled to Sepharose 4B as Substrate ,
Anal Biochem
 152 , 39 , 1986
Travis, J. and Roberts, R.
Human Trypsin. Isolation and Physical Chemical Characterization ,
Biochemistry
 8 , 2884 , 1969
Ueno, Y. and Morihara, K.
Use of Immobilized Trypsin for Semisynthesis of Human Insulin ,
Biotechnol Bioeng
 33 , 126 , 1989
van Gunsteren, W. and Karplus, M.
Protein Dynamics in Solution and in a Crystalline Environment: A Molecular Dynamics Study ,
Biochemistry
 21 , 2259 , 1982
Vandermeers, A. , Vanaermeers-Piret, M. , Rathe, J. and Christophe, J.
Substrate Activation of Rat Trypsins 1 and 2 ,
Arch Biochem Biophys
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Vandermeers, A. and Christophe, J.
Purification, Potential Enzymatic Activity and Amino Acid Composition of Chymotrypsinogen and Trypsinogens from Rat Pancreas. French ,
Biochim Biophys Acta
 188 , 101 , 1969
Vincent, J. , Lazdunski, M. and Delaage, M.
On the Use of Tetranitromethane as a Nitrate Reagent. The Reaction of Phenol Side-Chains in Bovine and Porcine Trypsinogens and Trypsins ,
Eur J Biochem
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Walde, P. , Peng, Q. , Fadnavis, N. , Battistel, E. and Luisi, P.
Structure and Activity of Trypsin in Reverse Micelles ,
Eur J Biochem
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Walker, J. and Keil, B.
Purification and Characterization of Different Active Forms of Pork Trypsin ,
Eur J Biochem
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Walsh, K. and Neurath, H.
Trypsinogen and Chymotrypsinogen as Homologous Proteins ,
Proc Natl Acad Sci U S A
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Walsh, K. , Kauffman, D. , Sampath Kumar, K. and Neurath, H.
On the Structure and Function of Bovine Trypsinogen and Trypsin ,
Proc Natl Acad Sci U S A
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Walsh, K.
Trypsinogens and Trypsins of Various Species , Methods in Enzymology Vol. 19 , G. Perlmann and L. Lorand , Academic Press, NY , 41 , 1970
Wang, D. , Wu, K. and Feinman, R.
Dissociability of Enzyme-alpha-2-Macro Globulin Complexes ,
Arch Biochem Biophys
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Wang, Q. , Zheng, Y. , Guo, X. and Wang, S.
Progressive Trypsin Digestion and Serum Inhibition in Articular Cartilage Monitored Using High-frequency Ultrasound in situ ,
Conf Proc IEEE Eng Med Biol Soc
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Watanabe, T. and Ogasawara, N.
Purification and Properties of Multiple Forms of Mouse Trypsinogen ,
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Trypsin Products

Description
Activity
Code
Cat. #
Size
Price
Description
SequENZ® Trypsin, Modified, Sequencing Grade
Source:
Bovine Pancreas
Trypsin, treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.
Store at -20°C. PROTECT FROM MOISTURE.
…
Ice Pack required
Activity
≥150 units per mg protein (at least 8,625 BAEE/2875 USP/NF units per mg protein)
Code
TRSEQZ
LS02120
4x25 µg
$98.00
LS02122
4x100 µg
$275.00
LS02123
1 mg
$500.00
LS02124
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 20000 x 1 ug. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
SequENZ® Trypsin, Modified, Sequencing Grade, Solution
Source:
Bovine Pancreas
Ready to use liquid preparation of Trypsin, treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity. Supplied as 1mgP/ml in 1.0mM HCl.
Store at 2-8°C.
…
Ice Pack required
Activity
---
Code
TRSEQZS
LS02150
250 ug
$130.00
LS02152
1000 ug
$415.00
LS02155
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 20000 x 1 ug. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin, Purified, Sequencing Grade II
Source:
Bovine Pancreas
Bovine trypsin that has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity and extensively purified to remove autolysis products. Supplied as a lyophilized powder.
Store at -20°C. PROTECT FROM MOISTURE.
…
Ice Pack required
Activity
≥150 units per mg protein (at least 8,625 BAEE/2875 USP/NF units per mg protein)
Code
TRSEQII
LS02115
4x25 µg
$88.00
LS02117
4x100 µg
$235.00
LS02119
1 mg
$420.00
LS02118
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 20000 x 1 µg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin, TPCK Treated
Source:
Bovine Pancreas
A chromatographically purified, diafiltered, lyophilized powder that has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity [Kostka, V., and Carpenter, F.: JBC, 239, 1799 (1964)].
Store at 2-8°C. PROTECT FROM MOISTURE.
…
Activity
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
Code
TRTPCK
LS003740
100 mg
$118.00
LS003741
500 mg
$420.00
LS003744
1 gm
$705.00
LS003742
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 20000 x 1 mg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin
Source:
Bovine Pancreas
Supplied as a chromatographically purified, diafiltered and lyophilized powder.
Store at 2-8°C. PROTECT FROM MOISTURE.
…
Activity
≥180 units per mg protein
Code
TRL3
LS003708
100 mg
$55.00
LS003707
1 gm
$340.00
LS003709
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 20000 x 1 mg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin
Source:
Bovine Pancreas
Supplied as a dialyzed and lyophilized powder.
Store at 2-8°C. PROTECT FROM MOISTURE.
…
Activity
≥180 units per mg protein
Code
TRL
LS003702
100 mg
$30.00
LS003703
1 gm
$160.00
LS003704
10 gm
$1,150.00
LS003706
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 200000 x 1 mg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin, TPCK-Treated, Irradiated
Source:
Bovine Pancreas
Chromatographically purified trypsin treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity according to Kostka, V., and Carpenter, F.H.: JBC, 239, 1799 (1964), Code: TRTPCK, lyophilized, irradiated and tested for the absence of mycoplasma and extraneous virus according to 9 CFR 113.53c. Each vial is filled to contain 100 mg.
Store at 2-8°C.
…
Activity
≥180 units per mg protein
Code
TRTVMF
LS003750
100 mg
$180.00
LS003752
5x100 mg
$725.00
Description
Trypsin, 2X, Sterile, Irradiated
Source:
Bovine Pancreas
Purified trypsin (Code: TRL), lyophilized, irradiated and tested for the absence of mycoplasma and extraneous virus according to 9 CFR113.53c. Each vial is filled to contain 100 mg.
Store at 2-8°C.
…
Activity
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
Code
TRLVMF
LS004454
100 mg
$116.00
LS004452
5x100 mg
$420.00
LS004458
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 10000 x 1 mg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
Description
Trypsin, 0.22µ Filtered
Source:
Bovine Pancreas
Trypsin chromatographically purified, diafiltered (Code TRL3) filtered thorugh a 0.22 micron pore size membrane and lyophilized in sterile vials. This product is not tested for pyrogenicity.
Store at 2-8°C.
…
Activity
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
Code
TRLS
LS003736
50 mg
$54.00
LS003734
5x50 mg
$235.00
LS003738
Bulk
---
The minimum amount for bulk packaging/pricing for this product is 100 x 50 mg. Please contact custservice@worthington-biochem.com to request a quote for smaller amounts.
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