Cyclic AMP independent protein kinase activity in rat cerebral cortex synaptic vesicles--partial characterization

The intrinsic protein kinase activity of a highly purified synaptic vesicle preparation was characterized. The time-course of the reaction was found to be rapid and linear for about 1 min, but plateaued after 30 min by which time approximately 1 nmol of 32P per mg protein was incorporated into trich...

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Bibliographic Details
Published in:Neurochemical research 1982-10, Vol.7 (10), p.1231-1242
Main Authors: Glaser, J, Weller, M G, Neethling, A C, Taljaard, J J
Format: Article
Language:English
Subjects:
Animals
Calcium - pharmacology
Cerebral Cortex - enzymology
Cyclic AMP - pharmacology
Female
Guanosine Triphosphate - metabolism
Hydrogen-Ion Concentration
Kinetics
Male
Neurotransmitter Agents - metabolism
Phosphorylation
Protein Kinases - analysis
Rats
Rats, Inbred Strains
Synaptic Vesicles - enzymology
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Summary:The intrinsic protein kinase activity of a highly purified synaptic vesicle preparation was characterized. The time-course of the reaction was found to be rapid and linear for about 1 min, but plateaued after 30 min by which time approximately 1 nmol of 32P per mg protein was incorporated into trichloroacetic acid precipitated vesicular protein. The enzyme was optimally active at pH 6.0 (37 degrees C), and had apparent Km values of 40 and 88 microM for ATP and GTP respectively. The enzyme was not stimulated by cAMP or cGMP. Mg2+ was required for maximal activity. The reaction was inhibited by free Ca2+, and non-selectively by Na+, K+, and NH4+.
ISSN:0364-3190
1573-6903
DOI:10.1007/BF00965894