Results 241 to 250 of about 11,445 (270)

Hybridization of Glyceraldehyde-3-phosphate Dehydrogenase in Borate

The Journal of Biochemistry, 1976
Conditions for the hybridization of glyceraldehyde-3-phosphate dehydrogenase (GPD) [EC 1.2.1.12] in the presence of dilute borate were examined with horseshoe crab and rabbit GPDs. Hybridization was strongly dependent upon pH, borate concentration, and temperature.
K, Suzuki, K, Hibino, K, Imahori
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Binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules

Molecular and Cellular Biochemistry, 1987
The interaction of glyceraldehyde 3-phosphate dehydrogenase with microtubules has been studied by measurement of the amount of enzyme which co-assembles with in vitro reconstituted microtubules. The binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules is a saturable process; the maximum binding capacity is about 0.1 mole of enzyme bound ...
C, Durrieu, F, Bernier-Valentin, B, Rousset   +2 more
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease

Pathologie Biologie, 2014
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme that catalyzes the sixth step of glycolysis and thus, serves to break down glucose for energy production. Beyond the traditional aerobic metabolism of glucose, recent studies have highlighted additional roles played by GAPDH in non-metabolic processes, such as control of gene ...
N, El Kadmiri, I, Slassi, B, El Moutawakil, S, Nadifi, A, Tadevosyan, A, Hachem, A, Soukri   +6 more
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1 Glyceraldehyde-3-phosphate Dehydrogenase

1976
Publisher Summary Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes reversibly the oxidation and phosphorylation of D-glyceraldehyde 3-phosphate (G-3P) to 1,3-diphosphoglycerate (DPGA). Glyceraldehyde-3-phosphate dehydrogenase occurs widely and abundantly throughout nature.
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Inactivation of glyceraldehyde-3-phosphate dehydrogenase by ferrylmyoglobin

Chemico-Biological Interactions, 1997
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was rapidly inactivated by ferrylmyoglobin (ferrylMb). FerrylMb rapidly reacts with the sulfhydryl group of protein. We therefore surmised that the cysteine residues of GAPDH react with ferrylMb. However, the amount of ferrylMb required to inactivate the enzyme was in excess of the equivalent amount of ...
T, Miura, S, Muraoka, T, Ogiso
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[Phosphorylation of glyceraldehyde-3-phosphate dehydrogenase].

Biokhimiia (Moscow, Russia), 1993
Phosphorylation of D-glyceraldehyde-3-phosphate dehydrogenase (GPDH) by Ca2+/phospholipid- and Ca2+/calmodulin-dependent protein kinases was shown to take place in rabbit skeletal muscle and brain extracts. The kinases could be "picked up" from the extract, using GPDH immobilized on CNBr-activated Sepharose 4B as an affinity adsorbent.
E A, Sergienko, A A, Ermakova, V I, Muronets, N K, Nagradova   +3 more
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[43] Glyceraldehyde 3-phosphate dehydrogenase—crystalline

1966
Publisher Summary This chapter discusses the determination of crystalline glyceraldehyde 3-phosphate dehydrogenase from human heart muscle and lobster tail muscle. In the case of determination of crystalline glyceraldehyde 3-phosphate dehydrogenase from human heart muscle, the enzyme is assayed spectrophotometrically as described for the lobster ...
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Glyceraldehyde-3-phosphate dehydrogenase mRNA

Journal of the Neurological Sciences, 1986
D.McEwen Nicholls, Krystyna Teichert-Kuliszewska, Maciej J. Kuliszewski   +2 more
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Glyceraldehyde-3-phosphate dehydrogenase

1993
Dietmar Schomburg, Margit Salzmann, Dörte Stephan   +2 more
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Glyceraldehyde-3-phosphate dehydrogenase (NADP+)

1993
Dietmar Schomburg, Margit Salzmann, Dörte Stephan   +2 more
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