The reactive site of human alpha 2-antiplasmin.
J Biol Chem
; 262(13): 6055-9, 1987 May 05.
Article
em En
| MEDLINE
| ID: mdl-2437112
ABSTRACT
Human alpha 2-antiplasmin rapidly forms a stable, equimolar complex with either its target enzyme, plasmin, or with trypsin. Perturbation of the inhibitor-trypsin complex results in peptide bond cleavage at the reactive site of the inhibitor with the concomitant release of a small peptide fragment which apparently represents the carboxyl-terminal segment of the inhibitor. Sequence analysis of this fragment, together with that of an overlapping peptide obtained by treatment of native inhibitor with either Staphylococcus aureus V8 proteinase or human neutrophil elastase, yields data which indicate that the reactive site of alpha 2-antiplasmin encompasses a P1-P'1 Arg-Met sequence. However, unlike alpha 1-1-proteinase inhibitor which has a Met residue in the P1-position, oxidation of alpha 2-antiplasmin has no effect on its inhibitory activity toward either plasmin, trypsin, or chymotrypsin, indicating the lesser mechanistic importance of the P'1-residue during enzyme inactivation by this inhibitor.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alfa 2-Antiplasmina
Limite:
Humans
Idioma:
En
Ano de publicação:
1987
Tipo de documento:
Article