Human plasma kallikrein
1974; Elsevier BV; Volume: 165; Issue: 1 Linguagem: Inglês
10.1016/0003-9861(74)90150-7
ISSN1096-0384
AutoresCláudio Luís Santos Sampaio, Show-Chu Wong, Elliott Shaw,
Tópico(s)Molecular Junctions and Nanostructures
ResumoA method is described for the convenient purification of the protease plasma kallikrein from human Cohn fraction IV-1. The enzyme was produced by endogenous activation after acid treatment to remove an inhibitor and was concentrated by the successive use of affinity adsorbents prepared by the immobilization of soybean trypsin inhibitor and aminobenzamidine. The esterase- and kinin-producing activities were enriched about 1100-fold from fraction IV-1. Several properties of plasma kallikrein strengthen the impression that it is related to trypsin, namely, competitive inhibition by benzamidine and the formation of a stable p-guanidinobenzoyl acyl enzyme intermediate. Inactivation by affinity labeling with Z-LysCH2Cl was successful in contrast to the inertness of Tos-LysCH2Cl.
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