Diphosphoinositide metabolism in bovine adrenal medulla

(1) A phosphatidylinositol kinase (EC 2.7.1.67) of a chromaffin vesicle membrane preparation isolated from bovine adrenal medulla was characterized. Its activity towards endogenous and exogenous phosphatidylinositol was very similar to the kinase activity of the microsomal fraction prepared from the...

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Bibliographic Details
Published inCanadian journal of biochemistry Vol. 54; no. 8; pp. 746 - 753
Main Authors Lefebvre, Y.A, White, D.A, Hawthorne, J.N
Format Journal Article
LanguageEnglish
Published Canada 01.08.1976
Subjects
Adrenal Medulla - enzymology
animal science
Animals
Binding Sites
Calcium - metabolism
Cattle
Cell Fractionation
Cytoplasmic Granules - metabolism
Kinetics
livestock
Membranes - enzymology
Microsomes - enzymology
Phosphatidylinositols - metabolism
Phosphotransferases - metabolism
Subcellular Fractions - enzymology
Surface-Active Agents - pharmacology
zoology
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Summary:(1) A phosphatidylinositol kinase (EC 2.7.1.67) of a chromaffin vesicle membrane preparation isolated from bovine adrenal medulla was characterized. Its activity towards endogenous and exogenous phosphatidylinositol was very similar to the kinase activity of the microsomal fraction prepared from the same tissue. (2) Phosphomonoesterase (EC 3.1.3.36) and diesterase activity hydrolysing membrane bound phosphatidylinositol 4-phosphate was located mainly in the microsomal fraction. No hydrolytic activity was present in the vesicle membrane. (3) Phosphorylation of chromaffin vesicle membrane phosphatidylinositol did not increase calcium-binding by the membranes.
ISSN:0008-4018
DOI:10.1139/o76-106