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J. Biochem, 1970, Vol. 68, No. 1 9-17
© 1970 Japanese Biochemical Society

research-article

Substrate Specificities of Kinin Releasing Enzymes: Hog Pancreatic Kallikrein and Snake Venom Kininogenase

Hisao KATO and Tomoji SUZUKI

The Division of Plasma Proteins, the Institute for Protein Research, Osaka University Osaka

1. Specific interactions of kinin releasing enzymes, pancreatic kallikrein [EC 3.4.4.21 [EC] ] and snake venom kininogenase with bovine kininogen-II (low molecular weight kininogen), both native and modified, were examined. Venom kininogenase liberated bradykinin from native kininogen-II and its reduced and S-carboxymeth-ylated derivatives. Hog pancreatic kallikrein, on the other hand, did not release kinin from modified kininogen-II's but liberated kallidin from the native bovine kininogen-II. Kallikrein and venom kininogenase cleaved the arginylseryl bond of the cyanogen bromide fragment containing the kinin moiety to liberate kallidin. From these results, it was assumed that a tertiary structure of the kininogen-II was required for the cleavage of the methionyl-lysyl bond to release kallidin by kallikrein, but not for the cleavage of the arginyl-seryl bond in the C-terminal part of the bradykinin sequence of kininogen-II.

2. Hog pancreatic kallikrein and venom kininogenase hydrolyzed poly-arginine, in addition to ar-N-tosyl-derivatives of arginine and lysine methylesters, but did not hydrolyze a-N-tosylmethionine ethylester appreciably. Kallikrein also attacked poly-lysine, although the venom kininogenase did not hydrolyze poly-lysine appreciably. Thus, there are some differences in the actions of kallikrein and venom kininogenase. Trypsin [EC 3.4.4.4 [EC] ] and plasmin [EC 3.4.4.14 [EC] ] hydrolyzed all the substrates mentioned above, except a-N-tosylmethionine methylester.


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