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Biochemical properties of rat protein kinase C-eta expressed in COS cells.

Authors: Dekker, LV  Parker, PJ  McIntyre, P 
Citation: Dekker LV, etal., FEBS Lett 1992 Nov 9;312(2-3):195-9.
Pubmed: (View Article at PubMed) PMID:1426252

Using a PKC-epsilon cDNA probe a cDNA for PKC-eta has been cloned from a rat lung cDNA library. When expressed in COS cells, rat PKC-eta appeared as an 84 kDa protein. PKC-eta expressed in COS cells, was solubilized by 1% Triton X-100 and purified away from the endogenous PKC-alpha by ammonium sulphate fractionation. The activity of this PKC-eta preparation was characterized with respect to cofactor dependence and substrate specificity. Various PKC pseudosubstrate peptides are phosphorylated by PKC-eta in a phospholipid and TPA-dependent but calcium-independent manner. The polypeptide histone IIIS is a poor substrate.


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CRRD Object Information
CRRD ID: 729427
Created: 2003-11-26
Species: All species
Last Modified: 2003-11-26
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.