Biochemical properties of rat protein kinase C-eta expressed in COS cells.
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.
Dekker
L V
LV
Sandoz Institute for Medical Research, London, UK.
Parker
P J
PJ
McIntyre
P
P
D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D007700:Kinetics; D008969:Molecular Sequence Data; D011493:Protein Kinase C / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity
D011493:Protein Kinase C; D000645:Ammonium Sulfate