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Characterization of human salivary kallikrein: reactivities to human plasma kininogens and proteinase inhibitors



Characterization of human salivary kallikrein: reactivities to human plasma kininogens and proteinase inhibitors



Journal of Biochemistry 93(3): 833-838



In order to clarify the enzymatic properties of human salivary kallikrein, its actions on human plasma kininogens and response to proteinase inhibitors were investigated. Salivary kallikrein released kinin from LMW [low-MW] and HMW [high-MW] kininogens, but acted preferentially on LMW kininogen. Salivary kallikrein did not completely release the kinin from HMW kininogen even after prolonged incubation (up to 60 min). The kinin releasing activity of salivary kallikrein was not inhibited by plasma proteinase inhibitors such as .alpha.2M[.alpha.2-macroglobulin], .alpha.2PI[.alpha.2-plasmin inhibitor], AT III [antithrombin III] and C1 INA [C1 inactivator] after preincubation for 60 min at 37.degree. C, but was inhibited progressively by .alpha.1-AT [.alpha.1-antitrypsin] as a function of preincubation time. SDS-PAGE [sodium dodecyl sulfate polyacrylamide gel electrophoresis] revealed that concomitantly with the progressive inhibition a new band of 92,000 daltons, which seemed to be a complex of salivary kallikrein and .alpha.1AT, was produced. The kininogen-depleted plasma inhibited the salivary kallikrein to the same degree as .alpha.1AT. Apparently, .alpha.1AT is the only inhibitor of salivary kallikrein in human plasma.

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Accession: 004928923

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PMID: 6553577

DOI: 10.1093/jb/93.3.833


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