Abstract
A search for tissue kallikreins in lower vertebrates resulted in the discovery of three novel kallikreins. Tissue kallikrein was isolated from the salivary gland of the Eastern Atlantic mole, Scalopus aquaticus, and the pancreas of the Southern frog, Rana berlandieri. A prokallikrein was identified in skeletal muscle of the black sea bass, Centropristis striata. These enzymes range in molecular mass from 27 to 36 kDa and are acidic proteins with pls between 4.2 and 5.3. Bass prokallikrein was activated by trypsin cleavage. These novel kallikreins were compared with human and rat tissue kallikreins in regard to immunoreactivity, molecular weight, isoelectric point, extinction coefficient, susceptibility to serine proteinase inhibitors and their ability to cleave low molecular weight dog kininogen to release kinin peptides.
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