Mammalian aldolases are isomer-selective high-affinity inositol polyphosphate binders
نویسندگان
چکیده
منابع مشابه
Subunit interaction in mammalian aldolases.
Enzyme inactivation was utilized to study subunit interaction in the homotetrameric glycolytic enzyme, aldolase. Isoenzymes from rabbit liver and skeletal muscle were inactivated in the presence of Pi and d-glyceraldehyde-P to a maximum stoichiometry of one modification per aldolase subunit. Subunit modification increased net negative charge on each subunit surface and was used to resolve modif...
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BACKGROUND Polyphosphate (a linear polymer of inorganic phosphate) is secreted from platelet dense granules, and we recently showed that it accelerates factor V activation by thrombin. OBJECTIVE To examine the interaction of polyphosphate with thrombin. METHODS AND RESULTS Thrombin, but not prothrombin, altered the electrophoretic migration of polyphosphate in gel mobility assays. Thrombin ...
متن کاملProperties of inositol polyphosphate 1-phosphatase.
We recently described inositol polyphosphate 1-phosphatase, an enzyme which cleaves the 1-phosphate from inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3) (Inhorn, R. C., and Majerus, P. W. (1987) J. Biol. Chem. 262, 15946-15952). We have now purified the enzyme to homogeneity from calf brain. The enzyme hydrolyzes 50.3 mumol of Ins(1,4)P2/min/mg protein. Th...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1986
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1986.tb10462.x