Results 21 to 30 of about 70 (68)
Some of the next articles are maybe not open access.
Immobilized hybrids of glyceraldehyde-3-phosphate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978Yeast 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 +2 more
openaire +2 more sources
β-Structure in glyceraldehyde-3-phosphate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract 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
openaire +2 more sources
Hybridization of Glyceraldehyde-3-phosphate Dehydrogenase in Borate
The Journal of Biochemistry, 1976Conditions 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
openaire +2 more sources
Binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules
Molecular and Cellular Biochemistry, 1987The 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 +2 more
openaire +2 more sources
On the ontogeny and interactions of glyceraldehyde-3-phosphate dehydrogenase
Mechanisms of Ageing and Development, 1986The interaction of GAPDH with cellular structure has been studied in the major tissues of the mouse during development. Overall the data provides a clear indication that interactions between GAPDH and cellular structure are appreciable in all major tissues, at least during early stages of development, and an analysis of the isozyme status of the enzyme
S, Reid, C, Masters
openaire +2 more sources
The Muridae glyceraldehyde-3-phosphate dehydrogenase family
Journal of Molecular Evolution, 1989Although 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 +4 more
openaire +2 more sources
Inactivation of glyceraldehyde-3-phosphate dehydrogenase by ferrylmyoglobin
Chemico-Biological Interactions, 1997Glyceraldehyde-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
openaire +2 more sources
Glyceraldehyde-3-Phosphate Dehydrogenase Inactivation by Peroxynitrite
Archives of Biochemistry and Biophysics, 1998Rabbit 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
openaire +2 more sources
Acyl Derivatives of Glyceraldehyde-3-Phosphate Dehydrogenase
Science, 1955Acetyl phosphate and 1,3-diphosphoglycerate react with glyceraldehyde-3-phosphate dehydrogenase to form relatively stable enzyme substrate compounds. These compounds appear to be thiol esters, and their properties indicate that they are intermediates in the catalytic activity of the enzyme: they undergo hydrolysis and arsenolysis in the presence of DPN
I, KRIMSKY, E, RACKER
openaire +2 more sources
The reaction of ozone with glyceraldehyde-3-phosphate dehydrogenase
Archives of Biochemistry and Biophysics, 1984Inactivation of glyceraldehyde-3-phosphate dehydrogenase (GPDH) by ozone can be correlated with oxidation of the active-site -SH residue. Oxidation of peripheral -SH groups, and tryptophan, methionine, and histidine residues occurs concomitantly, but loss of activity depends solely on active-site oxidation.
K L, Knight, J B, Mudd
openaire +2 more sources