Identification of the structures of multiple subspecies of protein kinase C expressed in rat brain.
Rat brain protein kinase C purified to apparent homogeneity [(1986) Biochem. Biophys. Res. Commun. 135, 636-643] was resolved into three distinct fractions, type I, II and III, upon chromatography on a hydroxyapatite column connected to high-performance liquid chromatography. Comparison of each fraction with the four subspecies of protein kinase C, that were separately expressed in COS cells transfected by the respective cDNAs, alpha, beta I, beta II and d gamma, identified the primary structures of these three fractions of protein kinase C. Type I corresponded to the enzyme encoded by the gamma-sequence; type II was a mixture of the two subspecies determined by the beta I- and beta II-sequences; and type III had the structure encoded by the alpha-sequence. The structures and properties of these subspecies of protein kinase C were similar to each other.
D000818:Animals; D001923:Brain Chemistry; D002851:Chromatography, High Pressure Liquid; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification*; D011493:Protein Kinase C / Q000235:genetics / Q000302:isolation & purification*; D051381:Rats; D011994:Recombinant Proteins / Q000235:genetics
D007527:Isoenzymes; D011994:Recombinant Proteins; D004247:DNA; D011493:Protein Kinase C