نتایج جستجو برای: phosphate dehydrogenase

تعداد نتایج: 163271  

Journal: :Cancer research 1971
G A Dunaway E C Smith

All of the glycolytic enzymes with the exception of enolase and phosphoglyceromutase were measured for WI-38, human embryonic lung tissue, and its SV40-transformed counterpart, WI-38VA13A. Also measured were glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and fructose 1,6-diphosphatase. Enzyme activity per IO6 cells indicated that glucose 6-phosphate deh...

Journal: :Applied and environmental microbiology 1977
R J Mehta L R Fare M E Shearer C H Nash

Mannitol kinase and mannitol-1-phosphate dehydrogenase activities were detected in two Micromonospora isolates. The presence of these enzyme activities indicates that mannitol is catabolized first to mannitol-1-phosphate and then to fructose-6-phosphate. Mannitol-oxidizing enzymes were also surveyed in representative species of four other genera of actinomycetes. Mannitol-1-phosphate dehydrogen...

Journal: :Plant physiology 1973
F Winkenbach C P Wolk

Preparations of heterocysts of Anabaena cylindrica Lemm. had 7- to 8-fold higher activities of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, 2-fold more hexokinase activity, and 0.02 to 0.06 times as much ribulose diphosphate carboxylase and glyceraldehyde 3-phosphate dehydrogenase activities as did whole filaments per milligram soluble protein in cell-free extracts. T...

2002
DAVID C. WHITE RONALD KABACK

Concentrative uptake of 16 amino acids by membrane vesicles isolated from Staphy2ococcus aureus is stimulated 3 to 100 times by the conversion of L-a-glycerol phosphate to dihydroxyacetone phosphate. With the exception of ascorbate-phenazine methosulfate, n-lactate, phosphoenolpyruvate, ATP, and a number of other metabolites and cofactors do not replace or-glycerol phosphate. Amino acid transpo...

Journal: :The Biochemical journal 1978
P H Sugden N J Hutson A L Kerbey P J Randle

The phosphorylation of sites additional to an inactivating site inhibits the formation of active pig heart pyruvate dehydrogenase complex from inactive pyruvate dehydrogenase phosphate complex by pig heart pyruvate dehydrogenase phosphate phosphatase.

Journal: :The Biochemical journal 1970
S J Ashcroft P J Randle

1. Glucose-phosphorylating and glucose 6-phosphatase activities, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADP(+)-linked isocitrate dehydrogenase, ;malic' enzyme and pyruvate carboxylase were assayed in homogenates of normal mouse islets. 2. Two glucose-phosphorylating activities were detected; the major activity had K(m) 0.075mm for glucose and was inhibited by gluc...

Journal: :The Journal of biological chemistry 1975
M Ray A Bhaduri

A new enzyme, galactose-6-phosphate dehydrogenase has been purified about 50-fold from goat liver. The enzyme can be distinguished from the nonspecific hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by its high substrate specificity and absolute pyridine nucleotide requirement. In contrast to the hexose-6-phosphate dehydrogenase, this enzyme is located exclusively in the...

Journal: :Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie 1979
A J Vermorken P Wirtz G T Spierenburg C A van Bennekom C H de Bruyn T L Oei

Kinetic properties of human hair root glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were studied in order to optimize the assay of these enzymes in lysates from single hair roots. In contrast to previously reported methods, an excess of purified 6-phosphogluconate dehydrogenase was added to the glucose-6-phosphate dehydrogenase reaction mixtures, thus allowing a more ex...

Journal: :The Journal of biological chemistry 2002
Emmanuelle Graciet Sandrine Lebreton Jean-Michel Camadro Brigitte Gontero

Glyceraldehyde 3-phosphate dehydrogenase and phosphoribulokinase exist as stable enzymes and as part of a complex in Chlamydomonas reinhardtii. We show here that phosphoribulokinase exerts an imprinting on glyceraldehyde 3-phosphate dehydrogenase, which affects its catalysis by decreasing the energy barrier of the reactions with NADH or NADPH by 3.8 +/- 0.5 and 1.3 +/- 0.3 kJ.mol(-1). Phosphori...

Journal: :The Journal of biological chemistry 1975
E J Hill T H Chou M C Shih J H Park

Glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde-3-phoshate:nicotinamide adenine dinucleotide oxidoreductase (phosphorylating), EC 1.2.1.12) forms a complex with 3-pyridinealdehyde-NAD which survives precipitation with 7% perchloric acid. The molar ratio bound 3-pyridinealdehyde-NAD to the enzyme is 2.5 to 2.9. Lactate, malate, and alcohol dehydrogenases do not form acid-precipitable ...

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