Trypsinogen - Manual

Trypsinogen has been shown to have certain intrinsic activity. See Knights and Light (1974) for further references. It is usually considered, however, as the inactive precursor of trypsin which may be activated by removal of a terminal hexapeptide to yield single-chain β-trypsin. Subsequent limited autolysis produces other active forms having two or more peptide chains bound by disulfide bonds. The predominant forms are α-trypsin, having two peptide chains and β-, a single chain. Different activity and thermal stability are shown by α- and β-trypsin.