The identification and purification of a mammalian- like protein kinase C in the yeast Saccharomyces cerevisiae
- 22 February 1991
- journal article
- research article
- Published by The Royal Society in Proceedings Of The Royal Society B-Biological Sciences
- Vol. 243 (1307) , 165-171
- https://doi.org/10.1098/rspb.1991.0027
Abstract
We have purified a yeast protein kinase that is phospholipid-dependent and activated by Diacylglycerol (DAG) in the presence of Ca$^{2+}$ 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
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