Conversion of protein kinase C from a Ca/sup 2 +/-dependent to an independent form of phorbol ester-binding protein by digestion with trypsin

Journal Article · Fri Aug 29 04:00:00 EDT 1986 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/S0006-291X(86)80116-4· OSTI ID:6937280

Huang, K P; Huang, F L

Tryptic fragments of protein kinase C containing the kinase (45 KDa) and phorbol ester-binding activity (38 KDa) were separated by Mono O column chromatography. The purified phorbol ester-binding fragment exhibits a higher affinity for phosphatidylserine than the native enzyme but comparable Kd for (/sup 3/H)phorbol 12,13-dibutyrate as the native enzyme. This proteolytic fragment binds phorbol ester equally efficient either in the presence or absence of Ca/sup 2 +/ and the addition of the kinase fragment did not restore the Ca/sup 2 +/-requirement for the binding. These results indicate that protein kinase C is composed of two functionally distinct units which can be expressed independently after limited proteolysis with trypsin.

• Research Organization: National Institute of Child Health and Human Development, Bethesda, MD
• OSTI ID: 6937280
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 1; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALKALINE EARTH METALS
ANIMALS
BIOCHEMICAL REACTION KINETICS
CALCIUM
CARCINOGENS
CHEMICAL BONDS
ELEMENTS
ENZYMES
ESTERS
HYDROLASES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MAMMALS
METALS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHORBOL ESTERS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
RATS
REACTION KINETICS
RODENTS
SERINE PROTEINASES
TRACER TECHNIQUES
TRANSFERASES
TRITIUM COMPOUNDS
TRYPSIN
VERTEBRATES