The identification and purification of a mammalian-like protein kinase C in the yeast Saccharomyces cerevisiae.
Proc Biol Sci
; 243(1307): 165-71, 1991 Feb 22.
Article
em En
| MEDLINE
| ID: mdl-1676520
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
Proteína Quinase C
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
Proc Biol Sci
Ano de publicação:
1991
Tipo de documento:
Article