Premium
Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca 2+ ‐inhibited protein kinase in rat brain
Author(s) -
Buday Lázló,
Mészáros György,
Farkas Gyöngyi,
Seprődi János,
Antoni Ferenc,
Faragó Anna
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80651-9
Subject(s) - oligopeptide , protein kinase a , biochemistry , chemistry , mitogen activated protein kinase kinase , protein kinase c , map2k7 , histone h1 , kinase , microbiology and biotechnology , peptide , isozyme , cyclin dependent kinase 9 , substrate (aquarium) , cgmp dependent protein kinase , c raf , cyclin dependent kinase 2 , enzyme , histone , biology , gene , ecology
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 Ca 2+ ‐inhibited protein kinase was also observed which was eluted from the hydroxyapatite column between type II and III isoenzymes of protein kinase C.