Results 231 to 240 of about 11,445 (270)

β-Structure in glyceraldehyde-3-phosphate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 1. 1. The secondary structure of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase ( d -glyceraldehyde-3-phosphate: NAD + oxidoreductase (phosphorylating), EC 1.2.1.12) appears to be predominately β-structure as judged by infrared absorption and circular dichroism.
D W, Darnall, T D, Barela
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The Radiolysis of Glyceraldehyde-3-phosphate Dehydrogenase

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1978
The yields in molecules per 100 eV for active-site and sulphydryl loss from glyceraldehyde-3-phosphate dehydrogenase have been determined in nitrous-oxide-saturated, aerated and argon-saturated solutions. Molecular hydrogen peroxide produces a sulphenic acid product, which can be repaired by post-irradiation treatment with dithiothreitol. Comparison of
J D, Buchanan, D A, Armstrong
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Glyceraldehyde-3-Phosphate Dehydrogenase Inactivation by Peroxynitrite

Archives of Biochemistry and Biophysics, 1998
Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was inactivated by peroxynitrite under biologically relevant conditions. The decrease of enzymatic activity followed an exponential function, and the concentration of peroxynitrite needed to inactivate 50% of 7 microM GAPDH (IC50) was 17 microM.
J M, Souza, R, Radi
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Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle

Nature, 1968
A unique amino-acid sequence for the polypeptide chain of pig muscle glyceraldehyde 3-phosphate dehydrogenase has been derived. This shows that the active enzyme contains four polypeptide chains of identical sequence and that there is a striking homology between the sequence of this enzyme and that of the same enzyme from lobster—a phylogenetically ...
J I, Harris, R N, Perham
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Immobilized hybrids of glyceraldehyde-3-phosphate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
Yeast glyceraldehyde-3-phosphate dehydrogenase (glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12) immobilized on CNBr-activated Sepharose 4-B has been subjected to dissociation to obtain matrix-bound dimeric species of the enzyme.
V I, Muronetz, R A, Asryants, N K, Nagradova   +2 more
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The Muridae glyceraldehyde-3-phosphate dehydrogenase family

Journal of Molecular Evolution, 1989
Although only one gene is known to be functional, numerous glyceraldehyde-3-phosphate dehydrogenase (GAPDH) related sequences are scattered throughout Mus musculus and Rattus rattus genomes. In this report we show that: (1) GAPDH pseudogenes are repeated to comparable extents, at least 400 copies, in 12 other Muridae species; (2) the complete, or ...
S, Riad-el Sabrouty, J M, Blanchard, L, Marty, P, Jeanteur, M, Piechaczyk   +4 more
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Immobilized flounder muscle glyceraldehyde 3-phosphate dehydrogenase

Molecular and Cellular Biochemistry, 1978
Partially purified flounder muscle (Pseudopleuronectus americanus) glyceraldehyde 3-phosphate dehydrogenase was immobilized on cyanogen bromide-activated Sepharose. The catalytic properties of the immobilized preparation were studied to determine if immobilization alters the kinetic properties of the native holoenzyme.
G, Spies-Karotkin, S M, Constantinides
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Enantiomeric specificity of glyceraldehyde 3-phosphate dehydrogenase

Archives of Biochemistry and Biophysics, 1978
Abstract Glyceraldehyde 3-phosphate dehydrogenase is selective for d -glyceraldehyde 3-phosphate but this stereoselectivity is not absolute. l -Glyceraldehyde 3-phosphate is also a substrate but the k cat K m value is at least 3 × 10 4 times smaller than that for the d -enantiomer.
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Hypoxic regulation of endothelial glyceraldehyde-3-phosphate dehydrogenase

American Journal of Physiology-Cell Physiology, 1998
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is induced by hypoxia in endothelial cells (EC). To define the mechanisms by which GAPDH is regulated by hypoxia, EC were exposed to cobalt, other transition metals, carbon monoxide (CO), deferoxamine, or cycloheximide in the presence or absence of hypoxia for 24 h, and GAPDH ...
K K, Graven, R J, McDonald, H W, Farber
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Sturgeon glyceraldehyde-3-phosphate dehydrogenase.

European journal of biochemistry, 1975
The formation of binary complexes between sturgeon apoglyceralddhyde-3-phosphate dehydrogenase, coenzymes (NAD+ and NADH) and substrates (phosphate, glyceraldehyde 3-phosphate and 1,3-bisphosphoglycerate) has been studied spectrophotometrically and spectrofluorometrica-ly.
N, Kelemen, N, Kellershohn, F, Seydoux
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