Ca super(2+)-calmodulin-dependent protein kinases Ia and Ib from rat brain. I. Identification, purification, and structural comparisons

Two Ca super(2+)-calmodulin (CaM)-dependent protein kinases were purified from rat brain using as substrate a synthetic peptide based on site 1 (site 1 peptide) of the synaptic vesicle-associated protein, synapsin I. One of the purified enzymes was an similar to 89% pure protein of M sub(r) = 43,000...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-01, Vol.267 (19), p.13460-13465
Main Authors: DeRemer, M F, Saeli, R J, Edelman, A M
Format: Article
Language:English
Subjects:
analysis
brain
calcium
calmodulin
identification
protein kinase
purification
rats
structure
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Summary:Two Ca super(2+)-calmodulin (CaM)-dependent protein kinases were purified from rat brain using as substrate a synthetic peptide based on site 1 (site 1 peptide) of the synaptic vesicle-associated protein, synapsin I. One of the purified enzymes was an similar to 89% pure protein of M sub(r) = 43,000 which bound CaM in a Ca super(2+)-dependent fashion. The other purified enzyme was an apparently homogenous protein of M sub(r) = 39,000 accompanied by a small amount of a M sub(r) = 37,000 form which may represent a proteolytic product of the 39-kDa enzyme. The 39-kDa protein bound CaM in a Ca super(2+)-dependent fashion. Gel filtration analysis indicated that both enzymes are monomers. The 43- and 39-kDa enzymes are named Ca super(2+)-CaM-dependent protein kinases Ia and Ib (CaM kinases Ia, Ib), respectively. Results indicate that CaM kinases Ia and Ib are distinct and possibly previously unrecognized enzymes.
ISSN:0021-9258