A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity.
FEBS Lett
; 215(2): 274-8, 1987 May 11.
Article
em En
| MEDLINE
| ID: mdl-3034666
ABSTRACT
A C-terminal fragment of an endogenous rabbit liver inhibitor for calcium-activated neutral protease (CANP) was produced in Escherichia coli and its inhibitory activity was examined after purification. The truncated inhibitor (373 amino acid residues), which contains two internal repeat structures, inhibits 2 mol CANP whereas the native liver inhibitor (639 residues), containing four internal repeat structures, inhibits 4 mol CANP. This supports the hypothesis that the repeating unit is the functional unit of inhibition. The results also indicate that post-translational modification of the inhibitor is not essential for inhibition.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Calpaína
/
Glicoproteínas
/
Escherichia coli
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1987
Tipo de documento:
Article