scholarly journals L-α-HYDROXY ACID OXIDASE ACTIVITY IN TETRAHYMENA

1967 ◽  
Vol 34 (3) ◽  
pp. 911-915 ◽  
Author(s):  
Michael R. Levy ◽  
Ann E. Hunt
Keyword(s):  
Oxidase Activity ◽  
Hydroxy Acid ◽  
Acid Oxidase

scholarly journals DISTRIBUTION OF PEROXISOMES (MICROBODIES) IN THE NEPHRON OF THE RAT

1969 ◽  
Vol 42 (2) ◽  
pp. 501-518 ◽  
Author(s):  
Margaret E. Beard ◽  
Alex B. Novikoff
Keyword(s):  
Light Microscopy ◽  
Electron Micrographs ◽  
Oxidase Activity ◽  
Hydroxy Acid ◽  
Acid Oxidase ◽  
Outer Medulla ◽  
Fixed Tissue ◽  
Low Levels ◽  
Proximal Convolution ◽  
Pars Convoluta

The distribution of peroxisomes (microbodies) in the rat nephron was studied cytochemically, using glutaraldehyde- or formaldehyde-fixed tissue, by means of α-hydroxy acid oxidase activity in light microscopy or oxidation of 3,3'-diaminobenzidine (DAB) at pH 9 in both light and electron microscopy.The two cytochemical methods show peroxisomes to be nearly sperical particles found only in cells of the proximal convoluted tubule. Lysosomes were identified in the same or parallel sections, with ß-glycerophosphate or 5'-cytidylic acid as substrate. They are found in all cells of the nephron. These cytochemical methods visualize the two organelles for light microscopy; they also permit unequivocal differentiation of all kidney peroxisomes from lysosomes in electron micrographs. Peroxisomes are larger and more reactive in the cells of the pars descendens (P3 segment) of the proximal convolution, located in the outer medulla and medullary rays, than in the cells of the pars convoluta (P1 and P2 segments), situated in the cortex. In contrast, lysosomes are much smaller in the P3 segment and larger and more reactive in the P1 and P2 segments. In all cells of the proximal convolution, peroxisomes tend to be concentrated nearer the base of the cells than do lysosomes. Mitochondria in P3 cells also show low levels of DAB oxidation at pH 6, in contrast to those in P1 and P2 cells. The possibility is discussed that P3 cells possess an extramitochondrial means of oxidation in which peroxisome oxidases play an important role.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

The Effect of Castration and Testosterone Propionate on d-Amino Acid Oxidase Activity in the Mouse

Science ◽  
1943 ◽  
Vol 98 (2534) ◽  
pp. 89-89
Author(s):  
L. C. Clark ◽  
C. D. Kochakian ◽  
R. Phyllis Fox
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Testosterone Propionate ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Polyphenolic inhibitors of alpha-acid oxidase activity

1988 ◽  
Vol 27 (1) ◽  
pp. 35-39 ◽  
Author(s):  
Elizabeth A. Williams ◽  
Robert C. Menary
Keyword(s):  
Oxidase Activity ◽  
Acid Oxidase

scholarly journals The localization of α-hydroxy acid oxidase in renal microbodies

1965 ◽  
Vol 160 (3) ◽  
pp. 329-344 ◽  
Author(s):  
John M. Allen ◽  
Margaret E. Beard ◽  
Skaidrite Kleinbergs
Keyword(s):  
Hydroxy Acid ◽  
Acid Oxidase

Presence of d-amino-acid oxidase protein in mutant mice lacking d-amino-acid oxidase activity

1991 ◽  
Vol 23 (11) ◽  
pp. 1301-1305 ◽  
Author(s):  
Konno Ryuichi ◽  
Yamamoto Katsuhiko ◽  
Niwa Akira ◽  
Yasumura Yosihiro
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Mutant Mice ◽  
Acid Oxidase ◽  
Amino Acid Oxidase
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