Glyceraldehyde-3-phosphate dehydrogenase, muscl

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]

The basis of the action of iodoacetate on muscle contraction was uncovered by Dickens and Rapkine (ca. 1933). They found iodoacetate alkylated SH groups on proteins, especially those in glyceraldehyde 3-phosphate dehydrogenase (G-3-PDH). When the enzyme was inhibited precursors accumulated—hexose mono- and diphosphates—as in Lundsgaard s experiments. [Pg.54]

Fig. 21. Chain trace of lobster muscle glyceraldehyde-3-phosphate dehydrogenase subunit. Stereo drawing from the work of Rossmann and colleagues [166]. Bound NAD is also shown.

Glyceraldehyde-3-phosphate dehydrogenase occurs widely and abundantly throughout nature. It comprises about 20% of the total soluble protein in yeast (10) and up to 10% of the soluble protein from muscle... [Pg.3]

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]

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

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]

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]

B-side Glyceraldehyde-3-phosphate dehydrogenase Lobster muscle s vn-NAD X-Ray 67... [Pg.337]

Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...