Isolation and properties of creatine kinase from the breast muscle of tropical fruit bat, Eidolon helvum (Kerr)

Publication Type:Journal Article
Year of Publication:1986
Authors:A. Afolayan, Daini O. A.
Journal:Comp. Biochem. Physiol. B
Volume:85
Pagination:463-468
Date Published:1986
Keywords:Chiroptera, Eidolon helvum, Nigeria, Pteropodidae, West Africa
Abstract:

1. Creatine kinase, from fruit bat breast muscle, has been purified to homogeneity.2. The mol. wt of the enzyme was estimated to be about 78,000-80,000 with two subunits of 42,500.3. There are nine thiol residues/mol of the enzyme and two of these react readily with DTNB leading to total inactivation of the enzyme.4. The metal ion specificity was in order Mg2+ > Zn2+ > Co2+.5. Initial velocity and product inhibition studies of the reverse reaction are consistent with sequential reaction but of either rapid equilibrium random or ordered type.

URL:Afolayan & Daini 1986.pdf http://dx.doi.org/10.1016/0305-0491(86)90028-3
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