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SOLUBILIZATION OF MEMBRANE ASSOCIATED PHOSPHATIDYLINOSITOL KINASE FROM SACCHAROMYCES CEREVISIAE
Author(s) -
MCKENZIE MAUREEN A.,
CARMAN GEORGE M.
Publication year - 1982
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1982.tb00297.x
Subject(s) - phosphatidylinositol , biochemistry , saccharomyces cerevisiae , glycerol , pi , solubilization , enzyme , kinase , chemistry , microsome , sodium , membrane , phosphorylation , chromatography , yeast , organic chemistry
ABSTRACT ATP: phosphatidylinositol (PI) 4‐phosphotransferase (PI kinase, EC 2.7.1.67) catalyzes the phosphorylation of PI to form PI 4‐monophosphate. A variety of solubilization agents were examined for their ability to release PI kinase from the microsomes of Saccharomyces cerevisiae. The most effective agent to solubilize the enzyme was sodium deoxycholate. Maximal solubilization was obtained with 1% sodium deoxycholate and 10 mM MgCl 2. A 2.3‐fold increase in specific activity was achieved with 91% of the activity solubilized. The sodium deoxycholate solubilized PI kinase remained at the top of a glycerol gradient whereas the membrane associated enzyme sedimented to the bottom of a glycerol gradient.