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Your search keyword '"Arginase metabolism"' showing total 11 results
Start Over Descriptor "Arginase metabolism" Language italian
11 results on '"Arginase metabolism"'

1. [The new role of an old enzyme, as studied by A. Clementi, in neurodegenerative diseases].

Author

Stella AM

Subjects
ATP Synthetase Complexes, Animals, Apoptosis physiology, Citrulline metabolism, Humans, Mitochondria genetics, Mitochondria physiology, Multienzyme Complexes metabolism, Neurodegenerative Diseases enzymology, Neurons metabolism, Nitric Oxide metabolism, Phosphotransferases (Phosphate Group Acceptor) metabolism, Arginase metabolism, Arginine metabolism, Neurodegenerative Diseases physiopathology, Nitric Oxide Synthase metabolism
Published
2000

3. [Subcellular localization of phosphate-dependent glutaminase in the chick kidney].

Author

Grillo MA

Subjects
Animals, Arginase metabolism, Kidney metabolism, Malate Dehydrogenase metabolism, Microsomes enzymology, Mitochondria enzymology, Subcellular Fractions metabolism, Chickens metabolism, Glutaminase metabolism, Kidney enzymology, Phosphates metabolism, Subcellular Fractions enzymology
Published
1977

4. [Metabolism of ornithine in human gingival tissue].

Author

Pinna GG, Chessa G, Luglié PF, Trova R, and Sisini A

Subjects
Gingiva enzymology, Gingivitis enzymology, Humans, In Vitro Techniques, Arginase metabolism, Collagen biosynthesis, Gingiva metabolism, Gingivitis metabolism, Ornithine-Oxo-Acid Transaminase metabolism, Proline biosynthesis, Transaminases metabolism
Abstract

The behavior of two enzymes of the ornithine pathway, leading to the formation of proline and, eventually, of collagen, arginase and ornithine oxo-acid aminotransferase has been investigated in normal and inflamed gingival tissue. Both enzymatic activities show a statistically significant decrease in pathological samples as compared to normal ones. The data on arginase activity may be in agreement with the already documented low level of urea in pathological gingival fluid, while a decrease of the ornithine aminotransferase activity could be linked to the phenomenon of gingival retraction, i.e. the lack of complete regeneration of gingival tissue usually observed in chronically inflamed subjects, that would be reasonably parallel to a decreased proline/collagen synthesis.

Published
1989

5. [Effect of environmental conditions on arginine metabolism in Helix vermiculata].

Author

Sisini A, Casolo Pernecco L, Naitana AL, and Pinna GG

Subjects
Animals, Arginase metabolism, Glutamate-Ammonia Ligase metabolism, Liver metabolism, Ornithine Carbamoyltransferase metabolism, Ornithine-Oxo-Acid Transaminase metabolism, Pancreas metabolism, Urea metabolism, Urease metabolism, Arginine metabolism, Helix, Snails metabolism
Published
1978

7. [Arginase characteristics in an ammoniotele].

Author

Sisini A, Pinna GG, and Virdis-Usai R

Subjects
Animals, Chromatography, Ion Exchange, Gills enzymology, Liver enzymology, Manganese metabolism, Muscles enzymology, Pancreas enzymology, Temperature, Arginase metabolism, Brachyura physiology
Abstract

Arginase (EC 3.5.3.1.) is active in the hepatopancreas, gills and pincer muscle of the ammoniotele Carcinus maenas. Its activity in the hepatopancreas is mainly localized in mitochondria. The enzyme becomes inactive at 37 degrees C if the assay is carried out without previous incubation with Mn2+; the optimum temperature for the fully activated enzyme is 47 degrees C. Two fractions showing arginase activity can be separated on DEAE-cellulose at pH 8.3, the most active being eluted by a linear gradient of KCl at a concentration of 0.3 divided by 0.4M, the other with a buffer front. Since ornithine transaminase (EC 2.6.1.13.) activity has been detected in the hepatopancreas, arginase activity in this organ is possibly related to ornithine catabolism leading to proline and glutamate.

Published
1981

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