Porcine pancreatic prokallikrein. III. Some different forms of kallikrein generated from prokallikrein.

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Abstract
Porcine pancreatic kallikreins generated from their precursors prokallikreins A and B in 3 different ways, i.e., kallikreins A and B obtained from autolyzed pancreas, kallikreins A'' and B'' spontaneously generated during the purification of prokallikreins A and B, and kallikreins A" and B" generated from purified prokallikreins A and B by treatment with trypsin, were each highly purified and their properties were compared. The Km values for BzArgOEt hydrolysis, the mobilities on immunoelectrophoresis and the elution profiles from a DEAE-Sepharose CL-6B column of kallikreins A'' and B'', and kallikreins A" and B" closely resembled each other but apparently differed from those of kallikreins A and B. Kallikreins A and B were confirmed to consist of 2 polypeptide chains (3 chains to some extent), while kallikreins A", B" and B'' were each determined to consist of a single chain. The amino acid compositions of the 2-chain kallikrein and the single-chain kallikrein were very similar, though somewhat higher values of Leu, Glu and Lys residues were observed in the single-chain kallikrein as compared with the 2-chain kallikrein. Kallikreins A" and B" generated from prokallikreins A and B by the action of trypsin were considered to be very similar to, or identical with kallikreins A'' and B'' spontaneously generated during the purification of prokallikreins A and B. Two-chain kallikreins A and B may be generated from single-chain kallikreins A" and B" by the action of some protease(s) other than trypsin during the autolysis process.

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