THE IDENTIFICATION AND PURIFICATION OF A MAMMALIAN-LIKE PROTEIN-KINASE-C IN THE YEAST SACCHAROMYCES-CEREVISIAE

被引：35
作者：
SIMON, AJ
MILNER, Y
SAVILLE, SP
DVIR, A
MOCHLYROSEN, D
ORR, E
机构：
[1] UNIV LEICESTER, DEPT GENET, ADRIAN BLDG, UNIV RD, LEICESTER LE1 7RH, ENGLAND
[2] HEBREW UNIV JERUSALEM, INST LIFE SCI, DEPT BIOL CHEM, MYERS SKIN BIOL & BIOCHEM LAB, IL-91904 JERUSALEM, ISRAEL
[3] UNIV CALIF SAN FRANCISCO, SAN FRANCISCO GEN HOSP, SCH MED, DEPT NEUROL & PHARMACOL, SAN FRANCISCO, CA 94110 USA
[4] UNIV CALIF SAN FRANCISCO, SAN FRANCISCO GEN HOSP, RES CTR, SAN FRANCISCO, CA 94110 USA
[5] UNIV CALIF SAN FRANCISCO, SAN FRANCISCO GEN HOSP, ERNEST GALLO CLIN, SAN FRANCISCO, CA 94110 USA
来源：
PROCEEDINGS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 1991年 / 243卷 / 1307期
关键词：
D O I：
10.1098/rspb.1991.0027
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
We have purified a yeast protein kinase that is phospholipid-dependent and activated by Diacylglycerol (DAG) in the presence of Ca2+ or by the tumour-promoting agent tetradecanoyl-phorbol acetate (TPA). The properties of this enzyme are similar to those of the mammalian protein kinase C (PKC). The enzyme was purified using chromatography on DEAE-cellulose followed by hydroxylapatite. The latter chromatography separated the activity to three distinguishable sub-species, analogous to the mammalian PKC isoenzymes. The fractions enriched in PKC activity contain proteins that specifically bind TPA, are specifically phosphorylated in the presence of DAG and recognized by anti-mammalian PKC antibodies.
引用
收藏
页码：165 / 171
页数：7
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