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 ◽  
...  
1985 ◽  
Vol 16 (6) ◽  
pp. 614-617
Author(s):  
Masakatsu NISHIKAWA ◽  
Hiroyoshi HIDAKA ◽  
Shigeru SHIRAKAWA ◽  
Robert S. ADELSTEIN

1992 ◽  
Vol 282 (1) ◽  
pp. 219-223 ◽  
Author(s):  
T Sassa ◽  
J Miwa

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.


Biochemistry ◽  
1992 ◽  
Vol 31 (2) ◽  
pp. 482-490 ◽  
Author(s):  
Takaomi C. Saido ◽  
Keiko Mizuno ◽  
Yasuhiko Konno ◽  
Shinichi Osada ◽  
Shigeo Ohno ◽  
...  

1997 ◽  
Vol 10 (1) ◽  
pp. 32-37 ◽  
Author(s):  
Martha Robles-Flores ◽  
Erika Rendón-Huerta ◽  
J.Adolfo Garcı́a-Sáinz

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