Results 21 to 30 of about 70 (68)

Inactivation of glyceraldehyde 3‐phosphate dehydrogenase by a bifunctional reagent [PDF]

FEBS Letters, 1969
openaire   +2 more sources

YEAST GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Journal of Biological Chemistry, 1953
Edwin G. Krebs, Gale W. Rafter, J. McBroom Junge   +2 more
openaire   +2 more sources

THE MECHANISM OF ACTION OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Journal of Biological Chemistry, 1954
openaire   +2 more sources

Some of the next articles are maybe not open access.

Related searches:

Glyceraldehyde 3-phosphate dehydrogenases

Journal of Molecular Biology, 1965
Publisher Summary This chapter discusses about glyceraldehyde 3-phosphate dehydrogenase. The subunit structure of several NAD-linked dehydrogenases is now well established. Comparison of the amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenases from different species is of interest from the point of view of three-dimensional structure and ...
J Ieuan Harris
exaly   +2 more sources

Human serine racemase is inhibited by glyceraldehyde 3-phosphate, but not by glyceraldehyde 3-phosphate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2021
Murine serine racemase (SR), the enzyme responsible for the biosynthesis of the neuromodulator d-serine, was reported to form a complex with glyceraldehyde 3-phosphate dehydrogenase (GAPDH), resulting in SR inhibition. In this work, we investigated the interaction between the two human orthologues. We were not able to observe neither the inhibition nor
Michielon A., Marchesani F., Faggiano S., Giaccari R., Campanini B., Bettati S., Mozzarelli A., Bruno S.   +7 more
openaire   +6 more sources

Inactivation of glyceraldehyde 3-phosphate dehydrogenase

Archives of Biochemistry and Biophysics, 1967
Abstract Enzymatic activity and physical chemical properties have been determined for yeast glyceraldehyde 3-phosphate dehydrogenase (GPD) exposed to low and high pH. Inactivation of the enzyme is rapid below pH 4.5 and above pH 11, and is accompanied by a decrease in sedimentation constant resulting in large part from dissociation into its ...
Y, Shibata, M J, Kronman
openaire   +2 more sources

Glyceraldehyde-3-phosphate dehydrogenase and apoptosis

Journal of Neuroscience Research, 2000
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as playing an integral role in glycolysis. During the past 20 years, however, a number of novel, additional functions for GAPDH have been described. These include acting as an uracil DNA glycosylase, activator of transcription, binding to RNA, and an involvement in tubulin ...
M D, Berry, A A, Boulton
openaire   +2 more sources

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
openaire   +2 more sources

Hybridization of Glyceraldehyde-3-phosphate Dehydrogenase

The Journal of Biochemistry, 1975
1. Glyceraldehyde-3-phosphate dehydrogenases [EC 1.2.1.12] from rabbit, pig, lobster, yeast, E. coli, and B. stearothermophilus have been subjected to hybridization in 3M NaCL. 2. Suitable mixtures of electrophoretically distinct glyceraldehyde-3-phosphate dehydrogenases were found to give five-membered by electrophoresis on cellulose acetate. 3.
K, Suzuki, J I, Harris
openaire   +2 more sources

Molecular Symmetry of Glyceraldehyde-3-phosphate Dehydrogenase

Journal of Molecular Biology, 1972
Abstract The rotation function has been used to determine the orientation of the molecule of lobster glyceraldehyde- 3-phosphate dehydrogenase in its crystal cell. The results have also established the 222 symmetry of the molecule. Comparison with the known structure of lactate dehydrogenase suggests structural similarities and indicates the relative
M G, Rossmann, G C, Ford, H C, Watson, L J, Banaszak   +3 more
openaire   +2 more sources