Physicochemical properties of non-activated and activated renin from human amniotic fluid.
Biochim Biophys Acta
; 569(2): 202-10, 1979 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-38848
ABSTRACT
The main physicochemical and enzymic properties of non-activated and activated human amniotic renin (EC 3.4.99.19) were studied in order to clarify the relationships between the two enzymes. Human amniotic renin was activated by dialysis against acidic buffer (pH 3.3), direct acidification or trypsin treatment. All procedures produced similar activation. The physicochemical characteristics of non-activated and activated renin were compared to those of human renal renin. Non-activated renin had a molecular weight of 45,500. A similar molecular weight was obtained by gel eluate activation and by acid treatment of renin prior to gel filtration. Similar isoelectric points were also found for non-activated and activated renin. One major renin peak focused at pH 6.6, whereas no similar renin peak was detected in extracts from normal human kidney. In addition, non-activated and activated renin forms were found to have the same optimal pH, the same Km and the same inhibiting pepstatin concentrations.
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Base de dados:
MEDLINE
Assunto principal:
Renina
/
Líquido Amniótico
Limite:
Female
/
Humans
/
Pregnancy
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1979
Tipo de documento:
Article