Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca2+‐inhibited protein kinase in rat brain

FEBS Letters

Seprődi, János¹  Antoni, Ferenc¹  Buday, Lázló¹  Mészáros, György¹  Faragó, Anna¹  Farkas, Gyöngyi¹ 

[1] 1st Institute of Biochemistry, Semmelweis University Medical School, PO Box 260, 1444 Budapest 8, Hungary

关键词: Protein kinase C;    Substrate specificity;    Synthetic oligopeptide substrate;    Isoenzyme;    Ca2+-inhibited enzyme;   

DOI  :  10.1016/0014-5793(89)80651-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The activities of rat brain protein kinase C isoenzymic fractions separated by hydroxyapatite chromatography were measured with histone H1 or the oligopeptide Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide as substrates. The oligopeptide was a better substrate than histone H1 for nearly all of the protein kinase C fractions. Two subtractions of type III isoenzyme were resolved (IIIa and IIIb); type IIIb was characterized by a very low histone kinase activity compared to its peptide kinase activity. In some brain extracts a phospholipid-dependent but Ca²⁺-inhibited protein kinase was also observed which was eluted from the hydroxyapatite column between type II and III isoenzymes of protein kinase C.

【 授权许可】

Unknown