Chromatographic resolution of altered forms of protein kinase C
Rapid chromatographic resolution of protein kinase C (PKC) in extracts of rat brain on DEAE-cellulose yielded two major peaks of activity. These fractions bound phorbol esters with identical affinity and specificity and had similar ratios of PKC to phorbol ester-binding activities. Chicken egg yolk antibodies raised to PKC in the first fraction reacted with 74 to 76 kilodalton peptides in the second fraction. Chromatography of each fraction on hydroxylapatite yielded similar distributions of three PKC isozymes. Rechromatography of the DEAE-cellulose fractions on DEAE-cellulose confirmed that these forms of PKC were not rapidly interconvertible. Results of experiments in which extracts or fractions were incubated with MgATP and phosphatase inhibitors were consistent with elution of dephospho-PKC in the first fraction while the second fraction contained phospho-PKC. If confirmed, this suggests that a substantial fraction of PKC in rat and mouse tissues exists in the phosphorylated form.
- Research Organization:
- Purdue Univ., West Lafayette, IN
- OSTI ID:
- 6150539
- Report Number(s):
- CONF-870644-
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
- Country of Publication:
- United States
- Language:
- English
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PHORBOL ESTERS
BIOLOGICAL EFFECTS
ENZYME ACTIVITY
PHOSPHOTRANSFERASES
BIOCHEMICAL REACTION KINETICS
BRAIN
CHROMATOGRAPHY
RATS
RESOLUTION
ANIMALS
BODY
CARCINOGENS
CENTRAL NERVOUS SYSTEM
ENZYMES
ESTERS
KINETICS
MAMMALS
NERVOUS SYSTEM
ORGANIC COMPOUNDS
ORGANS
PHOSPHORUS-GROUP TRANSFERASES
REACTION KINETICS
RODENTS
SEPARATION PROCESSES
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560300* - Chemicals Metabolism & Toxicology