Peroxisomal Oxidases and Their Probable Role in Controlling Animal Metabolism

[1]  G. A. Hamilton,et al.  The reaction of oxalyl thiolesters with nucleophiles, especially thiols☆ , 1986 .

[2]  G. A. Hamilton,et al.  The nonenzymic hydrolysis of Δ2-thiazoline-2-carboxylate: The product of the suspected physiological reaction catalyzed by d-amino acid oxidase , 1986 .

[3]  G. A. Hamilton,et al.  Inhibition of the catalytic subunit of phosphorylase phosphatase by oxalyl thioesters and its possible relevance to the mechanism of insulin action. , 1986, Biochemical and biophysical research communications.

[4]  P. Lazarow,et al.  Flux of palmitate through the peroxisomal and mitochondrial beta-oxidation systems in isolated rat hepatocytes. , 1985, Biochimica et biophysica acta.

[5]  D. Price,et al.  On the mechanism of regulation of type I phosphoprotein phosphatase from bovine heart. Regulation by a novel intracyclic activation-deactivation mechanism via transient phosphorylation of the regulatory subunit by phosphatase-1 kinase (FA). , 1985, The Journal of biological chemistry.

[6]  E. Brush,et al.  Equilibrium constants for the formation of glyoxylate thiohemiacetals and kinetic constants for their oxidation by O2 catalyzed by l-hydroxy acid oxidase☆ , 1985 .

[7]  G. A. Hamilton,et al.  Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase. , 1984, Biochemical and biophysical research communications.

[8]  C. Y. Huang,et al.  On the mechanism of activation of the ATP X Mg(II)-dependent phosphoprotein phosphatase by kinase FA. , 1984, The Journal of biological chemistry.

[9]  W. Parks,et al.  Insulin stimulation of hepatic malic enzyme activity in normal and diabetic rats controlled by different regulatory processes. , 1983, The Journal of biological chemistry.

[10]  S. Markey,et al.  Biosynthesis of S-methyl-N-oleoylmercaptoethylamide from oleoyl coenzyme A and S-adenosylmethionine. , 1982, The Journal of biological chemistry.

[11]  C. Kahn,et al.  Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine. , 1982, The Journal of biological chemistry.

[12]  G. A. Hamilton,et al.  The inhibition of mammalian d-amino acid oxidase by metabolites and drugs. Inferences concerning physiological function , 1982 .

[13]  C. Kahn,et al.  Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system , 1982, Nature.

[14]  N. Naber,et al.  Inhibition of dopamine β-hydroxylase by thiazoline-2-carboxylate, a suspected physiological product of D-amino acid oxidase , 1982 .

[15]  H. S. Mason,et al.  Oxidases and Related Redox Systems , 1982 .

[16]  E. Brush,et al.  THIOL‐GLYOXYLATE ADDUCTS AS SUBSTRATES FOR RAT KIDNEY L‐α‐HYDROXY ACID OXIDASE * , 1982 .

[17]  H. Osmundsen.  PEROXISOMAL βT‐OXIDATION OF LONG FATTY ACIDS: EFFECTS OF HIGH FAT DIETS * , 1982 .

[18]  G. A. Hamilton,et al.  Implications Concerning the Physiological Function of D-Amino Acid Oxidase as Derived from Inhibition Studies , 1982 .

[19]  G. A. Hamilton,et al.  Reactions of cysteamine and other amine metabolites with glyoxylate and oxygen catalyzed by mammalian D-amino acid oxidase. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[20]  R. Mellgren,et al.  Purification and properties of bovine myocardial phosphorylase phosphatase (protein phosphatase C). , 1978, Archives of biochemistry and biophysics.

[21]  E. Kun,et al.  Enzymatic degradation of succinyl-coenzyme A by rat liver homogenates. , 1978, Biochimica et biophysica acta.

[22]  W. Cleland,et al.  Inhibition and alternate-substrate studies on the mechanism of malic enzyme. , 1977, Biochemistry.

[23]  C. Duve,et al.  A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[24]  R. Y. Hsu,et al.  Mechanism of pigeon liver malic enzyme. Modification of sulfhydryl groups by 5,5'-dithiobis(2-nitrobenzoic acid) and N-ethylmaleimide. , 1974, The Journal of biological chemistry.