نتایج جستجو برای: phosphate dehydrogenase

تعداد نتایج: 163271  

Journal: :Postgraduate Medical Journal 1994

Journal: :Journal of Biological Chemistry 1953

Journal: :Journal of Biological Chemistry 1961

Journal: :Journal of Medical Case Reports 2008
Gladys Cossio de Gurrola Juan José Araúz Elfilda Durán Maribel Aguilar-Medina Rosalío Ramos-Payán Noemí García-Magallanes Gerardo Vaca Pacheco Eliakym Arámbula Meraz

INTRODUCTION Glucose-6-phosphate dehydrogenase deficiency is an X-linked recessive disease that causes acute or chronic hemolytic anemia and potentially leads to severe jaundice in response to oxidative agents. This deficiency is the most common human innate error of metabolism, affecting more than 400 million people worldwide. CASE PRESENTATION Here, we present the first documented case of k...

Journal: :The Biochemical journal 1972
A A Malcolm M G Shepherd

1. Glucose 6-phosphate dehydrogenase was isolated and partially purified from a thermophilic fungus, Penicillium duponti, and a mesophilic fungus, Penicillium notatum. 2. The molecular weight of the P. duponti enzyme was found to be 120000+/-10000 by gelfiltration and sucrose-density-gradient-centrifugation techniques. No NADP(+)- or glucose 6-phosphate-induced change in molecular weight could ...

2014
Alparslan Merdin Fatma Avci Nihal Guzelay

Red blood cells carry oxygen in the body and Glucose-6-Phosphate Dehydrogenase protects these cells from oxidative chemicals. If there is a lack of Glucose-6-Phosphate Dehydrogenase, red blood cells can go acute hemolysis. Convulsion is a rare presentation for acute hemolysis due to Glucose-6-Phosphate Dehydrogenase deficiency. Herein, we report a case report of a Glucose-6-Phosphate Dehydrogen...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1970
O Wieland E Siess

Pyruvate dehydrogenase from pig heart exists in active and inactive forms. Interconversion from the active (dephospho) form into the inactive (phospho) form is catalyzed by an ATP-dependent kinase. Conversely the enzyme is reactivated by a phosphatase which removes the phosphate group from the protein. By gradient centrifugation pyruvate dehydrogenase was prepared free of phosphatase but still ...

Journal: :The Journal of biological chemistry 1985
L McAlister M J Holland

Utilizing yeast strains containing insertion mutations in each of the three glyceraldehyde-3-phosphate dehydrogenase structural genes, the level of expression of each gene was determined in logarithmically growing cells. The contribution of the TDH1, TDH2, and TDH3 gene products to the total glyceraldehyde-3-phosphate dehydrogenase activity in wild type cells is 10-15, 25-30, and 50-60%, respec...

2005
B. F. DIXON MICHAEL J. SPARKES

Analogues of dihydroxyacetone phosphate and of 3-phosphoglycerate were made in which the phosphate group, -O-PO3H2, is replaced by the phosphonomethyl group, -CH2-PO3H2. The analogue of dihydroxyacetone phosphate is a substrate for aldolase and glycerol 1-phosphate dehydrogenase (Stribling, 1974), but not for triose phosphate isomerase. The analogue of 3-phosphoglycerate oxidizes NADH under the...

Journal: :Biochimica et biophysica acta 1975
R J Pollock A K Hajra B W Agranoff

Rates of phosphatidate synthesis from dihydroxyacetone phosphate via acyl dihydroxyacetone phosphate or glycerol phosphate are compared in homogenates of 13 tissues, most of which are deficient in glycerol phosphate dehydrogenase (EC 1.1.1.8). In all tissues examined, dihydroxyacetone phosphate entered phosphatidate more rapidly via acyl dihydroxyacetone phosphate than via glycerol phosphate. T...

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