scholarly journals Purification and characterization of protein kinase C from the nematode Caenorhabditis elegans

1992 ◽  
Vol 282 (1) ◽  
pp. 219-223 ◽  
Author(s):  
T Sassa ◽  
J Miwa
Keyword(s):  
Protein Kinase C ◽  
Caenorhabditis Elegans ◽  
Protein Kinase ◽  
Column Chromatography ◽  
Purification And Characterization ◽  
C Elegans ◽  
Kinase C ◽  
Sds Page ◽  
Cytosolic Extract

Protein kinase C (PKC) of Caenorhabditis elegans was identified by enzymatic activity and [3H]phorbol 12,13-dibutyrate binding after DEAE-Sephacel column chromatography of a crude cytosolic extract. Ca(2+)-dependent activation of nematode PKC was observed in the presence of phosphatidylserine. The enzyme was maximally activated by 1,2-dioleoylglycerol or phorbol 12-myristate 13-acetate in the presence of phosphatidylserine and Ca2+. Hydroxyapatite column chromatography showed only one peak of PKC activity with histone H1 and myelin basic protein as substrates. The enzyme was purified to near homogeneity by sequential chromatography on polylysine-agarose and phosphatidylserine affinity columns. The purified protein showed a molecular mass of 79 kDa on SDS/PAGE. The substrate specificity of the C. elegans enzyme was shown to be different from that of mammalian PKCs. Here we describe some of the properties of the nematode enzyme.

scholarly journals Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1

1995 ◽  
Vol 309 (1) ◽  
pp. 315-320 ◽  
Author(s):  
R H Palmer ◽  
P J Parker
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Limited Proteolysis ◽  
Purification And Characterization ◽  
Kinase C ◽  
Apparent Homogeneity ◽  
Physiological Relevance ◽  
Sds Page

The recently described protein kinase C-related kinase (PRK) family is comprised of at least three members: PRK1, PRK2 and PRK3. Here the expression, purification and characterization of the ubiquitously expressed isoform, PRK1, is described. The enzyme was expressed in COS 7 cells and subsequently purified to apparent homogeneity by sequential column chromatography. The purified PRK1 protein migrates as a single 120 kDa polypeptide on SDS/PAGE. It displays a substrate specificity that in part resembles that of protein kinase C (PKC); however, unlike PKC, it is not activated by any combination of phorbol esters, diacylglycerol and Ca2+. Nevertheless, it can be activated by limited proteolysis, indicating a negative regulatory role for the N-terminal domain(s). PRK1 is also activated by phospholipids. The physiological relevance of this activation is discussed.

Purification and Characterization of Protein Kinase C from a Higher Plant, Brassica campestris L

1994 ◽  
Vol 203 (1) ◽  
pp. 311-318 ◽  
Author(s):  
T. Nanmori ◽  
W. Taguchi ◽  
M. Kinugasa ◽  
Y. Oji ◽  
S. Sahara ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Brassica Campestris ◽  
Purification And Characterization ◽  
Higher Plant ◽  
Kinase C

scholarly journals Purification and characterization of Ca2+phospholipid dependent protein kinase (C kinase) from human platelets.

1985 ◽  
Vol 16 (6) ◽  
pp. 614-617
Author(s):  
Masakatsu NISHIKAWA ◽  
Hiroyoshi HIDAKA ◽  
Shigeru SHIRAKAWA ◽  
Robert S. ADELSTEIN
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Platelets ◽  
Purification And Characterization ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein

scholarly journals Molecular evidence for the direct involvement of a protein kinase C in developmental and behavioural susceptibility to tumour-promoting phorbol esters in Caenorhabditis elegans

1995 ◽  
Vol 312 (1) ◽  
pp. 69-74 ◽  
Author(s):  
Y Tabuse ◽  
T Sano ◽  
K Nishiwaki ◽  
J Miwa
Keyword(s):  
Protein Kinase C ◽  
Caenorhabditis Elegans ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Kinase Domain ◽  
Molecular Evidence ◽  
Wild Type ◽  
C Elegans ◽  
Kinase C ◽  
Tumour Promoters

The nematode Caenorhabditis elegans displays developmental and behavioural sensitivity to tumour-promoting phorbol esters. This sensitivity involves the gene tpa-1, which encodes two protein kinase C isoforms, TPA-1A and TPA-1B. Here we report the molecular nature of the sensitivity in this animal. Characterization of transposon Tc1-induced phorbol ester-resistant mutants has revealed that Tc1 was inserted in a region encoding the kinase domain, resulting in the loss of tpa-1 products. Introduction of a genomic DNA containing the entire wild-type tpa-1 locus into a Tc1-inserted mutant restored the sensitivity to tumour promoters, and tpa-1 products were also produced. These results suggest that the function of wild-type TPA-1 is necessary and sufficient for tumour promoters to cause developmental and behavioural sensitivity in C. elegans.

Purification and characterization of protein kinase C .epsilon. from rabbit brain

Biochemistry ◽  
1992 ◽  
Vol 31 (2) ◽  
pp. 482-490 ◽  
Author(s):  
Takaomi C. Saido ◽  
Keiko Mizuno ◽  
Yasuhiko Konno ◽  
Shinichi Osada ◽  
Shigeo Ohno ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rabbit Brain ◽  
Purification And Characterization ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Purification and Characterization of Receptors for Activated Protein Kinase C from Rat Hepatocytes

1997 ◽  
Vol 10 (1) ◽  
pp. 32-37 ◽  
Author(s):  
Martha Robles-Flores ◽  
Erika Rendón-Huerta ◽  
J.Adolfo Garcı́a-Sáinz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Hepatocytes ◽  
Purification And Characterization ◽  
Kinase C
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