Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Bloxham, D.P., and Cooper, C.K. (1982) Formation of a polymethylene bis(disulfide) inter-subunit crosslink between cys-281 residues in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase using octamethylene bzs-(methane[35]thiosulfonate). Biochemistry 21, 1807. [Pg.1048]

Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (MW = 140,000) catalyzes the oxidation and phosphorylation of glyceraldehyde-... [Pg.65]

Maximum rates and Km values were recently reported for seven aldehydes as substrates of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase 51). Values for which might have provided further evidence for the conclusion that the mechanism is ordered, were not reported, however. [Pg.24]

Dissociation Constants foe Coenzyme Compounds op Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase... [Pg.43]

On the other hand, a number of native proteins tested were found to be better substrates for cathepsin M than for cathepsin B (Table IV). Muscle and liver aldolases were inactivated by cathepsins M and B at comparable rates (Table IV) but yeast glucose-6-phosphate dehydrogenase was inactivated much more rapidly by cathepsin M and neither rabbit liver pyruvate kinase nor rabbit muscle glyceraldehyde-3-phosphate dehydrogenase was inactivated on incubation with cathepsin B. [Pg.84]

Kress Y, Gaskin F, Brosnan CF, Levine S (1981) Effects of zinc on the cytoskeletal proteins in the central nervous system of the rat. Brain Res 220 139-149 Krotkiewska B, Banas T (1992) Interaction of Zn2+ and Cu2+ ions with glyceraldehyde-3-phosphate dehydrogenase from bovine heart and rabbit muscle. Int J Biochem 24 1501-1505... [Pg.688]

Sergienko EA, Kharitonenkov AI, Bulargina TV et al (1992) D-glyceraldehyde-3-phosphate dehydrogenase purified firom rabbit muscle contains phosphotyrosine. FEBS Lett 304l21-23... [Pg.23]

Glyceraldehyde-3-phosphate dehydrogenase Origin rabbit muscle Biozyme... [Pg.1476]

Glyceraldehyde-3-phosphate Dehydrogenase Origin rabbit muscle Fluka... [Pg.1476]

For glyceraldehyde-3-phosphate dehydrogenase, conflicting conclusions have been reached by different workers (47 49). From one analysis of initial rate data, for the pig muscle enzyme, it appears that with glycer-aldehyde as substrate the mechanism is random (SO), whereas with glyceraldehyde 3-phosphate there is random combination of this substrate and NAD followed by phosphate as the compulsory third substrate (48). On the other hand, inhibition studies with the rabbit muscle enzyme indicate an ordered mechanism in which NAD is the first and acyl acceptor the last substrate to combine (51). More detailed comparative initial rate studies with the several aldehydes w hich act as substrates (Section II,E), preferably by a fluorimetric method (11,47), and isotope exchange studies at equilibrium are needed for this enzyme. [Pg.15]

The role of DIP in the thermostabilization of enzymes remains questionable. This solute was shown to have a positive effect on the stabilization of glyceraldehyde-3-phosphate dehydrogenase, but did not increase the stability of hydrogenase and pyruvate ferredoxin oxidoreductase of Thermotoga maritima or rabbit muscle lactate dehydrogenase. ... [Pg.312]

CoRi, G. T., Slein, M. W. and Cori, C. F. (1948) Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. J. Biol. Chem. 173, 605. [Pg.44]

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