Abstract:
:A new multifunctional protein kinase, which normally exists as an inactive form in the soluble fraction in mammalian tissues, attaches to membranes to exhibit full enzymatic activity. A low concentration of Ca2+ is absolutely necessary for this activation. This process is reversible. cAMP shows no effect. The active factors in membranes are phosphatidylinositol, phosphatidylserine, phosphatidic acid, diphosphatidylglycerol, and phosphatidylethanolamine in that order. Phosphatidylcholine and sphingomyelin are far less effective. Cytoplasmic as well as other membrane fractions from various tissues are active in supporting the enzymatic activity. A possible role of this Ca2+ and phospholipid-activated protein kinase system in transmembrane control is proposed.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Takai Y,Kishimoto A,Iwasa Y,Kawahara Y,Mori T,Nishizuka Y,Tamura A,Fujii Tdoi
10.1093/oxfordjournals.jbchem.a132557subject
Has Abstractpub_date
1979-08-01 00:00:00pages
575-8issue
2eissn
0021-924Xissn
1756-2651journal_volume
86pub_type
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