scholarly journals Purification and properties of arginase of rat kidney

1973 ◽  
Vol 133 (4) ◽  
pp. 779-788 ◽  
Author(s):  
George A. Kaysen ◽  
Harold J. Strecker
Keyword(s):  
Rat Liver ◽  
Rat Kidney ◽  
Mitochondrial Fraction ◽  
Tissue Extracts ◽  
Low Concentrations ◽  
Purification And Properties ◽  
Hydrolysis Rates ◽  
Kidney Enzyme ◽  
Acetone Treatment ◽  
Unknown Factor

l-Arginase from rat kidney was partially purified and some properties were compared with those of l-arginase of rat liver. The kidney enzyme was firmly bound to the mitochondrial fraction and after solubilization required arginine or an unknown factor in tissue extracts for stabilization after dialysis. The two enzymes differed also in stability with respect to acetone treatment, heating or freezing. In further contrast with liver arginase, arginase from kidney was not adsorbed to CM-cellulose at pH7.5 and its activity was not increased by incubation with Mn2+. Other differences were seen in relative specificities for substrates, ratio of hydrolysis rates with high and low concentrations of arginine and effects of certain inhibitors. Antisera prepared to pure liver arginase did not cross-react with partially purified kidney arginase.

scholarly journals Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney

1989 ◽  
Vol 261 (3) ◽  
pp. 761-768 ◽  
Author(s):  
D R Deshmukh ◽  
S M Mungre
Keyword(s):  
Rat Kidney ◽  
Deae Cellulose ◽  
Dicarboxylic Acids ◽  
Structural Similarity ◽  
Appreciable Amount ◽  
Kinetic Properties ◽  
Bovine Kidney ◽  
Purification And Properties ◽  
Kidney Enzyme ◽  
Structural Differences

Previous studies with rat kidney preparations indicated that 2-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are properties of a single protein. We found that bovine kidney contains an appreciable amount of AadAT activity, but lacks KAT activity. AadAT from bovine and rat kidney extracts were purified to electrophoretic homogeneity. The purification procedure included fractionation with (NH1)2SO1, heat treatment, DEAE-cellulose chromatography and hydroxyapatite chromatography. Physical and kinetic properties, such as pH optima, Km for substrates, Mr, electrophoretic mobility and inhibition by dicarboxylic acids of bovine kidney AadAT, were similar to those of the rat kidney enzyme. However, bovine kidney AadAT differed from rat kidney AadAT in substrate specificity, amino acid composition and stability when stored. The titration curve of bovine kidney AadAT was also different from that of the rat kidney enzyme. The results suggest that bovine kidney AadAT may have some structural similarity to rat kidney AadAT and that the structural differences observed between the two enzymes may explain the absence of KAT activity in bovine kidney.

scholarly journals Biochemical effects of the hypoglycaemic compound pent-4-enoic acid and related non-hypoglycaemic fatty acids. Carbohydrate metabolism

1968 ◽  
Vol 110 (3) ◽  
pp. 521-527 ◽  
Author(s):  
A. E. Senior ◽  
H. S. A. Sherratt
Keyword(s):  
Rat Liver ◽  
Rat Kidney ◽  
Enoic Acid ◽  
Rat Tissues ◽  
Pentanoic Acid ◽  
Kidney Slices ◽  
Biochemical Effects ◽  
Low Concentrations ◽  
Cyclopropanecarboxylic Acid ◽  
Cyclobutanecarboxylic Acid

1. The effects of the hypoglycaemic compound, pent-4-enoic acid, and of four structurally related non-hypoglycaemic compounds (pent-2-enoic acid, pentanoic acid, cyclopropanecarboxylic acid and cyclobutanecarboxylic acid), on glycolysis, glucose oxidation and gluconeogenesis in some rat tissues were determined. 2. None of the compounds at low concentrations inhibited glycolysis by particle-free supernatant fractions from rat liver, skeletal muscle and intestinal mucosa, though there was inhibition by cyclopropanecarboxylic acid and cyclobutanecarboxylic acid at 3mm concentration. 3. Pent-4-enoic inhibited the oxidation of [1−14C]palmitate by rat liver slices, but did not increase the oxidation of [U−14C]glucose. 4. Pent-4-enoic acid (0·01mm) strongly inhibited gluconeogenesis by rat kidney slices from pyruvate or succinate, but none of the other compounds inhibited significantly at low concentrations. 5. There was also some inhibition of gluconeogenesis in kidney slices from rats injected with pent-4-enoic acid. 6. The mechanism of the hypoglycaemic effect of pent-4-enoic acid is discussed; it is suggested that there is an inhibition of fatty acid and ketone-body oxidation and of gluconeogenesis so that glucose reserves become exhausted, leading to hypoglycaemia. 7. The mechanism of the hypoglycaemic action of pent-4-enoic acid appears to be similar to that of hypoglycin.

scholarly journals Purification and Properties of Rat Liver Tyrosine Aminotransferase

1969 ◽  
Vol 244 (13) ◽  
pp. 3618-3624 ◽  
Author(s):  
F A Valeriote ◽  
F Auricchio ◽  
G M Tomkins ◽  
D Riley
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Purification And Properties

Purification and properties of a neutral protease from rat liver chromatin

Biochemistry ◽  
1974 ◽  
Vol 13 (25) ◽  
pp. 5128-5134 ◽  
Author(s):  
Ming Ta Chong ◽  
William T. Garrard ◽  
James Bonner
Keyword(s):  
Rat Liver ◽  
Neutral Protease ◽  
Purification And Properties ◽  
Liver Chromatin
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