Lactoperoxidase - Manual

Lactoperoxidase (LPO) catalyzes the hydrogen peroxide oxidation of iodide.

The bovine milk enzyme is identical to that formed in bovine lacrimal and salivary glands (Morrison et al. 1965; and Morrison and Allen, 1963). It is possible that LPO may be important in controlling bacterial flora (Bjorck et al. 1970; Gothefors and Marklund, 1975; and Morrison and Allen, 1966). LPO is useful for labelling proteins with radioiodine (Gow and Wardlaw 1975; Holohan et al. 1973; Morrison and Bayse 1973; Bayse et al. 1972; Frantz and Turkington 1972; and Marchalonis 1969). For membrane studies the large LPO molecule limits labelling to the exposed surface. Poduslo and Braun (1975) report on the topography of membrane proteins of the myelin sheath. Shin and Carraway (1974) and Phillips and Morrison (1971) report on erythrocyte and Nachman et al. (1973) on platelet membranes. Haustein (1975) studied the cell-surface protein of lymphoma cells and Huber et al. (1975) mitochondrial membranes. Chloroplast membranes were reported on by Arntzen et al. (1974). Jone and Hager (1976), and Hogg (1974) compare membrane protein of normal and transformed cell. Immobilized LPO has also proven of interest (Johnson et al. 1975; Karonen et al. 1975; and David 1972).

Characteristics of Lactoperoxidase from Bovine Milk: