Isolation and properties of creatine kinase from the breast muscle of tropical fruit bat, Eidolon helvum (Kerr).
Comp Biochem Physiol B
; 85(2): 463-8, 1986.
Article
em En
| MEDLINE
| ID: mdl-3780189
ABSTRACT
Creatine kinase, from fruit bat breast muscle, has been purified to homogeneity. The mol. wt of the enzyme was estimated to be about 78,000-80,000 with two subunits of 42,500. There are nine thiol residues/mol of the enzyme and two of these react readily with DTNB leading to total inactivation of the enzyme. The metal ion specificity was in order Mg2+ greater than Zn2+ greater than Co2+. Initial velocity and product inhibition studies of the reverse reaction are consistent with sequential reaction but of either rapid equilibrium random or ordered type.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Quirópteros
/
Creatina Quinase
/
Músculos
Limite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B
Ano de publicação:
1986
Tipo de documento:
Article