Physical properties of a purified cyclic adenosine 3': 5' monophosphate dependent protein kinase from bovine heart muscle

J. Erlichman, C. S. Rubin, O. M. Rosen

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

The physical properties of a homogeneous preparation of cyclic adenosine 3':5' monophosphate (cyclic AMP) dependent protein kinase and its subunits were studied using gel filtration, sucrose density gradient sedimentation, and analytical ultracentrifugation. Molecular weights of the holoenzyme and its cyclic AMP binding and phosphotransferase (catalytic) components were 174,000, 98,000, and 38,000, respectively. Frictional and axial ratios were 1.6 and 12 for both the holoenzyme and the cyclic AMP binding protein and 1.1 and 3 for the catalytic component. It is concluded that the native enzyme is composed of two catalytic units and one cyclic AMP binding protein containing two polypeptide chains of equal size.

Original languageEnglish (US)
Pages (from-to)7607-7609
Number of pages3
JournalJournal of Biological Chemistry
Volume248
Issue number21
StatePublished - 1973

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Adenosine
Protein Kinases
Muscle
Myocardium
Physical properties
Holoenzymes
Carrier Proteins
Ultracentrifugation
Sedimentation
Gel Chromatography
Sucrose
Phosphotransferases
Molecular Weight
Gels
Molecular weight
Peptides
Cyclic AMP
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Physical properties of a purified cyclic adenosine 3' : 5' monophosphate dependent protein kinase from bovine heart muscle. / Erlichman, J.; Rubin, C. S.; Rosen, O. M.

In: Journal of Biological Chemistry, Vol. 248, No. 21, 1973, p. 7607-7609.

Research output: Contribution to journalArticle

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