Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Leonard A. Fahien"'
Publikováno v:
Diabetes
Leucine is the only physiologic amino acid that can stimulate insulin release by itself, and a great deal of evidence suggests that leucine does this by allosterically activating glutamate dehydrogenase (GDH). GDH catalyzes the oxidative deamination
Publikováno v:
Diabetes. 51:2669-2676
Nutrient secretagogues can increase the production of succinyl-CoA in rat pancreatic islets. When succinate esters are the secretagogue, succinyl-CoA can be generated via the succinate thiokinase reaction. Other secretagogues can increase production
Autor:
Tatyana Budker, José I. Laboy, Prakash Prabhakar, Zafeer Z. Din, Leonard A. Fahien, Michael C. Chobanian
Publikováno v:
Archives of Biochemistry and Biophysics. 364:185-194
At the normal pH of the cytosol (7.0 to 7.1) and in the presence of physiological (1.0 mM) levels of free Mg2+, the Vmax of the NADPH oxidation is only slightly lower than the Vmax of NADH oxidation in the cytosolic glycerol-3-phosphate dehydrogenase
Publikováno v:
Journal of Biological Chemistry. 268:17935-17942
Although pyruvate carboxylase associated with both mitochondrial aspartate aminotransferase and malate dehydrogenase, it had a higher affinity for the amino-transferase. Furthermore, the aminotransferase enhanced dissociation of malate dehydrogenase
Autor:
Leonard A. Fahien, J K Teller
Publikováno v:
Journal of Biological Chemistry. 267:10411-10422
The level of aspartate aminotransferase in liver mitochondria was found to be approximately 140 microM, or 2-3 orders of magnitude higher than its dissociation constant in complexes with the inner mitochondrial membrane and the high molecular weight
Publikováno v:
Journal of Biological Chemistry. 267:10423-10432
Kinetic studies of Morris 7777 hepatoma mitochondrial NAD(P) malic enzyme were consistent with an ordered mechanism where NAD adds to the enzyme before malate and dissociation of NADH from the enzyme is rate-limiting. In addition to its active site,
Autor:
Susan M. Moran, Debbie McKenzie, H C Towle, Michael J. MacDonald, Leonard A. Fahien, T M Walker, J H Kaysen
Publikováno v:
Journal of Biological Chemistry. 266:1335-1340
Much evidence has accumulated to support the idea that leucine can stimulate insulin release by allosterically activating glutamate dehydrogenase thus enhancing glutamate metabolism. It is less clear how the metabolism of leucine itself contributes t
Publikováno v:
Journal of Biological Chemistry. 265:19486-19494
The inner mitochondrial membranes from bovine heart, rat liver, and Morris hepatoma 7777 all bound the mitochondrial isozymes of aspartate aminotransferase and malate dehydrogenase with comparable affinities and binding ratios (mg of enzyme bound per
Publikováno v:
American Journal of Physiology-Endocrinology and Metabolism. 259:E548-E554
Agents that stimulate insulin release from fresh pancreatic islets were tested for their ability to capacitate pancreatic islets to secrete insulin and to support beta-cell survival in tissue culture. Capacitation was defined as the ability to releas
Publikováno v:
Archives of Biochemistry and Biophysics. 279:104-108
Glyceraldehyde phosphate, a glycolytic intermediate, and succinic acid (as its methyl ester to make it permeable to the cell), a citric acid cycle intermediate, were the only glucose metabolites of many recently tested that stimulated insulin release