The identification and purification of a mammalian-like protein kinase C in the yeast Saccharomyces cerevisiae. |
| |
Authors: | A J Simon Y Milner S P Saville A Dvir D Mochly-Rosen E Orr |
| |
Institution: | Department of Genetics, University of Leicester, U.K. |
| |
Abstract: | 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. |
| |
Keywords: | |
|
|