[Some properties of peptidase from rat heart, breaking down luliberin]. / Nekotorye svoistva peptidazy iz serdtsa krysy, rasshchepliaiushchei liuliberin.
Biokhimiia
; 48(8): 1384-9, 1983 Aug.
Article
em Ru
| MEDLINE
| ID: mdl-6354276
The properties of rat heart peptidase hydrolyzing luliberin were studied. This peptidase was shown to be a sulfhydryl metalloenzyme with m.w. of about 100000. The maximal enzyme activity was observed at neutral values of pH Ca2+ (5 X 10(-6) M) increased the enzyme activity by 50%, thus being indicative of an anomalous dependence of the enzyme activity of substrate concentration. At luliberin concentrations of 10(-7)-10(-6) M the enzyme activation by Ca2+ was considerably reduced and returned to the initial level when the peptide concentration was increased up to 10(-5) M. It was assumed that the peptidase under study is a regulatory enzyme whose activity depends on concentrations of Ca2+ and of the reaction substrate, luliberin.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeo Hidrolases
/
Hormônio Luteinizante
/
Miocárdio
Limite:
Animals
Idioma:
Ru
Revista:
Biokhimiia
Ano de publicação:
1983
Tipo de documento:
Article
País de publicação:
Federação Russa