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Title: Chromatographic resolution of altered forms of protein kinase C

Abstract

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.

Authors:
; ; ;
Publication Date:
Research Org.:
Purdue Univ., West Lafayette, IN
OSTI Identifier:
6150539
Report Number(s):
CONF-870644-
Journal ID: CODEN: FEPRA
Resource Type:
Conference
Journal Name:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
Additional Journal Information:
Journal Volume: 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
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; 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; TRANSFERASES; VERTEBRATES; 560300* - Chemicals Metabolism & Toxicology

Citation Formats

Ashendel, C L, Minor, P L, Baudoin, P A, and Carlos, M. Chromatographic resolution of altered forms of protein kinase C. United States: N. p., 1987. Web.
Ashendel, C L, Minor, P L, Baudoin, P A, & Carlos, M. Chromatographic resolution of altered forms of protein kinase C. United States.
Ashendel, C L, Minor, P L, Baudoin, P A, and Carlos, M. 1987. "Chromatographic resolution of altered forms of protein kinase C". United States.
@article{osti_6150539,
title = {Chromatographic resolution of altered forms of protein kinase C},
author = {Ashendel, C L and Minor, P L and Baudoin, P A and Carlos, M},
abstractNote = {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.},
doi = {},
url = {https://www.osti.gov/biblio/6150539}, journal = {Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)},
number = ,
volume = 46:6,
place = {United States},
year = {Fri May 01 00:00:00 EDT 1987},
month = {Fri May 01 00:00:00 EDT 1987}
}

Conference:
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