Results 201 to 210 of about 10,324 (247)

Butane-2,3-diacetals of Glyceraldehyde: A Stable Alternative to Glyceraldehyde Acetonide

Angewandte Chemie - International Edition, 2002
Steven V Ley
exaly   +3 more sources

Development of a Method for Quantitation of Glyceraldehyde in Various Body Compartments of Rodents and Humans

Journal of Agricultural and Food Chemistry, 2021
There is limited information available about the physiological content of glyceraldehyde, a precursor of toxic advanced glycation end products. The conventional derivatization method for aldoses using 1-phenyl-3-methyl-5-pyrazolone did not allow ...
Yasuki Matsumura, Kaori Ikeda, Nobuya Inagaki   +2 more
exaly   +2 more sources

Glyceraldehyde-3-Phosphate, a Glycolytic Intermediate, Plays a Key Role in Controlling Cell Fate Via Inhibition of Caspase Activity

Molecules and Cells, 2009
Glyceraldehyde-3-phosphate is a key intermediate in several central metabolic pathways of all organisms. Aldolase and glyceraldehyde-3-phosphate dehydrogenase are involved in the production or elimination of glyceraldehyde-3-phosphate during glycolysis ...
Sang J Chung, Sunghyun Kang, Sayeon Cho   +2 more
exaly   +2 more sources

Glyceraldehyde; an X-ray study of DL-glyceraldehyde dimer

Journal of the Chemical Society, Chemical Communications, 1973
An X-ray study of DL-glyceraldehyde, dimerized by hemiacetal bondings, shows that the molecule has a chair-form symmetrical p-dioxan structure with all the hydroxy and hydroxymethyl groups bonded equatorially; the conformation is similar to that of β-D-glucopyranose.
Masanori Senma, Zenei Taira, Kenji Osaki, Tooru Taga   +3 more
openaire   +1 more source

Reductive metabolism of D-glyceraldehyde, L-glyceraldehyde and dihydroxyacetone in rat liver

International Journal of Biochemistry, 1976
Abstract 1. 1. The paper describes NADH- and NADPH-dependent enzyme activities in rat liver which catalyse the reduction of the following substrates: d -glyceraldehyde, l -glyceraldehyde and dihydroxyacetone. Test conditions for the optimal rates of the oxidoreductase reactions are described. 2. 2.
Marco Feraudi, Günter Schmolz
openaire   +1 more source

Glyceraldehyde and the Pancreatic β-Cell

1997
D-glyceraldehyde is commonly used as a stimulus of insulin release from the pancreatic β-cell1–3. It is generally accepted that the triose can be metabolized in the β-cell via the glycolytic pathway, thus stimulating insulin release in a manner analogous to glucose1–3.
Best, L, Elliott, A C, Davies, J
openaire   +3 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

Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde

Analytical Biochemistry, 1984
Glyceraldehyde reacts with hemoglobin S in the intact erythrocyte to reduce the degree of polymerization, thereby inhibiting sickling of the erythrocyte. Only five of the 24 amino groups per alpha beta dimer react with glyceraldehyde; the adducts are present as ketoamine structures, formed by Amadori rearrangement of the initial Schiff base adducts on ...
A S, Acharya, L G, Sussman, W M, Jones, J M, Manning   +3 more
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

Thermophilic Glyceraldehyde-3-P Dehydrogenase

1976
D-Glyceraldehyde-3-P:NAD oxidoreductase (phosphorylating) (E.C. 1.2.1.12) (abbr. GPDH) is a ubiquitous enzyme, found in most living systems, where it functions in the glycolytic pathway. There were several reasons for studying the enzyme in thermophilic bacteria.
R E, Amelunxen, R, Singleton
openaire   +2 more sources