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Isozymes of pyruvate kinase in vertebrates: their physical, chemical, kinetic and immunological properties.
  • E. Hall, G. Cottam
  • Biology, Medicine
  • The International journal of biochemistry
  • 1978
The physical, chemical, immunologie and kinetic properties of the four isozymes of pyruvate kinase are tabulated, finding the L- and R-isozymes are kinetically similar and immunologically cross-reactive with the M 1 -isozyme. Expand
Measurement of gluconeogenesis and pyruvate recycling in the rat liver: a simple analysis of glucose and glutamate isotopomers during metabolism of [1,2,3‐13C3]propionate
The 13C spectra of glucose collected from rats after gastric versus intravenous administration of [1,2,3‐13C3]propionate indicated that pyruvate recycling was slightly higher in vivo (49%) while glucose production was unchanged, indicating that a direct measure of gluconeogenesis and pyruVate recycling may be obtained from a single 13C‐NMR spectrum of blood collected after oral administration of enriched propionate. Expand
The sulfhydryl groups of citrate cleavage enzyme.
Chicken liver citrate cleavage enzyme has an apparent optimum activity at pH 8.7, similar to the enzyme isolated from rat liver, and the loss of enzyme activity observed upon storage and its subsequent reactivation by dithiothreitol does not result from changes in aggregation and dissociation of the enzyme as judged by gel electrophoresis and ultracentrifugation. Expand
Plasma and erythrocyte lipids in sickle cell anaemia.
The content and composition of plasma and erythrocyte lipids from individuals having sickle cell anaemia has been determined and significant decreases in cholesterol and phospholipid were observed in LDL and HDL. Expand
Glycosylation of LDL decreases its ability to interact with high-affinity receptors of human fibroblasts in vitro and decreases its clearance from rabbit plasma in vivo.
It is speculated that pathologic levels of plasma glucose in vivo could result in a decrease in LDL uptake as a result of glycosylation of LDL, which could contribute to hypercholesterolemia and its pathophysiology. Expand
A study of the mechanism of O-phosphorylhydroxylamine synthesis catalyzed by pyruvate kinase.
It is proposed that bicarbonate and hydroxylamine occupy the pyruvate-binding site of the enzyme and that Zn++ or Mn++ ions form a complex with the nitrogen atom of hydroxyamine, thereby polarizing the N—O bond and increasing the likelihood of a nucleophilic attack on the terminal phosphorus atom of adenosine triphosphate. Expand
Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4+ and CD8+ spleen T cells.
Exogenous methionine enkephalin incubated with CD4+ or CD8+ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC, aExpand
The pathogenesis of abnormal erythrocyte morphology in burns.
The ratio of free fatty acids to albumin in the plasma was greatly increased throughout and may have a primary role in the abnormal erythrocyte morphology and decreased half-life in burned patients. Expand
Proton relaxation and kinetic studies of ternary complexes of an allosteric pyruvate kinase from yeast.
The ternary complexes of Mn2+-yeast pyruvate kinase formed upon addition of substrates, products, and the activator fructose 1,6-diphosphate were investigated by proton relaxation rate measurements and kinetic studies and it is suggested that the allosteric activator functions primarily by modifying the carboxyl subsite of P-enolpyruvates and thereby raises the affinity of the enzyme for the substrate. Expand
Methionine enkephalin metabolism by murine macrophage ectopeptidase(s)
Ectopeptidases which hydrolyze opioid and other neuropeptides have been identified in brain, kidney and intestine. In this study, identification of the enzymes metabolizing the opioid peptideExpand