Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II.

Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Research Abstract Details 

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Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Abstract Text:

H Sato,T Yamauchi,H Fujisawa,

A calmodulin-dependent protein kinase has been purified from rat spleen. The enzyme showed a remarkably similar substrate specificity and kinetic parameters to those of rat brain calmodulin-dependent protein kinase II, and exhibited cross-reactivity to a monoclonal antibody against rat brain calmodulin-dependent protein kinase II, indicating that the enzyme might be a calmodulin-dependent protein kinase II isozyme. The sedimentation coefficient was 13.9S, the Stokes radius was 67 A, and the molecular weight was calculated to be 380,000. The purified enzyme gave five polypeptides bands, corresponding to molecular weights of 51,000, 50,000, 21,000, 20,000, and 18,000, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Incubation of the purified enzyme with Ca2+, calmodulin, and ATP under phosphorylating conditions induced the phosphorylation of all five polypeptides. When the logarithm of the velocity of the phosphorylation was plotted against the logarithm of the enzyme concentration (van't Hoff plot), slopes of 0.89, 0.94, and 1.1 were obtained for the phosphorylation of the 50/51-kDa doublet, 20/21-kDa doublet, and 18-kDa polypeptide, respectively. These results indicate that the phosphorylation of the five polypeptides is an intramolecular process, and further indicate that all five polypeptides are subunits of this enzyme. Of the five polypeptides, only the 50- and 51-kDa polypeptides bound to [125I]calmodulin, the other polypeptides not binding to it. A number of isozymic forms of calmodulin-dependent protein kinase II so far demonstrated in various tissues are known to be composed of subunits with molecular weights of 50,000 to 60,000 which can bind to calmodulin. Thus a new type of calmodulin-dependent protein kinase II was demonstrated in the present study.

Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Publishing Authors By Initials

H Sato,T Yamauchi,H Fujisawa,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 107

Page Numbers: 802-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1990

Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II. Information

Substance Name: Calcium-Calmodulin-Dependent Protein Kin

Registry Number: EC 2.7.11.17

Grant and Affiliation Information for Purification and characterization of calmodulin-dependent protein kinase II from rat spleen: a new type of calmodulin-dependent protein kinase II.

AFFILIATION: Department of Biochemistry, Asahikawa Medical College, Hokkaido.

Country: JAPAN

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MEDLINETA: J Biochem

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