Cytochemical localization by ferricyanide reduction of ?-hydroxy acid oxidase activity in peroxisomes of rat kidney

1971 ◽  
Vol 27 (2) ◽  
pp. 137-158 ◽  
Author(s):  
T. K. Shnitka ◽  
G. G. Talibi
Keyword(s):  
Oxidase Activity ◽  
Hydroxy Acid ◽  
Rat Kidney ◽  
Acid Oxidase ◽  
Ferricyanide Reduction ◽  
Cytochemical Localization

THIOL-GLYOXYLATE ADDUCTS AS SUBSTRATES FOR RAT KIDNEY L-?-HYDROXY ACID OXIDASE

1982 ◽  
Vol 386 (1 Peroxisomes a) ◽  
pp. 422-425 ◽  
Author(s):  
Edward J. Brush ◽  
Gordon A. Hamilton
Keyword(s):  
Hydroxy Acid ◽  
Rat Kidney ◽  
Acid Oxidase

Molecular forms of l-α-hydroxy acid oxidase from rat kidney

1973 ◽  
Vol 321 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Carlos E. Domenech ◽  
Estela E. Machado De Domenech ◽  
Antonio Blanco
Keyword(s):  
Hydroxy Acid ◽  
Rat Kidney ◽  
Molecular Forms ◽  
Acid Oxidase

Crystal Structure Analysis of Recombinant Rat Kidney Long Chain Hydroxy Acid Oxidase†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (5) ◽  
pp. 1521-1531 ◽  
Author(s):  
Louise M. Cunane ◽  
John D. Barton ◽  
Zhi-wei Chen ◽  
K. H. Diêp Lê ◽  
David Amar ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Hydroxy Acid ◽  
Rat Kidney ◽  
Crystal Structure Analysis ◽  
Acid Oxidase ◽  
Long Chain

scholarly journals D-aspartate oxidation by rat and bovine renal peroxisomes: an electron microscopic cytochemical study.

1990 ◽  
Vol 38 (9) ◽  
pp. 1377-1381 ◽  
Author(s):  
M E Beard
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Electron Microscopic Level ◽  
Acid Oxidase ◽  
Electron Microscopic ◽  
Amino Acid Oxidase ◽  
Cytochemical Localization ◽  
Peroxisomal Enzyme ◽  
Cytochemical Study ◽  
Biochemical Studies

D-amino acid oxidase, a peroxisomal enzyme, and D-aspartate oxidase, a potential peroxisomal enzyme, share biochemical attributes. Both produce hydrogen peroxide in flavin-requiring oxidative reactions. Such similarities suggest that D-aspartate oxidase may also be localized to peroxisomes. Definitive identification of D-aspartate oxidase as a peroxisomal enzyme depends, however, on visualization at the electron microscopic level. Using incubation conditions shown to be specific for the enzyme in biochemical studies, this report extends the cytochemical localization of D-amino acid oxidase to bovine renal peroxisomes, and shows that D-aspartate can be oxidized by rat and bovine renal peroxisomes. An unexpected finding was the sensitivity of both D-amino acid oxidase activity (proline specific) and D-aspartate oxidase activity to inhibition by agents used in biochemical studies to discriminate between the two enzyme activities. Therefore, it is possible that, in the cytochemical system used in this study, (a) either D-proline and D-aspartate are substrates for only one enzyme or (b) the two enzymes have additional overlapping biochemical properties.

Mechanistic studies on the rat kidney flavoenzyme L-α-hydroxy acid oxidase

Biochemistry ◽  
1975 ◽  
Vol 14 (15) ◽  
pp. 3482-3490 ◽  
Author(s):  
Thomas H. Cromartie ◽  
Christopher Walsh
Keyword(s):  
Hydroxy Acid ◽  
Rat Kidney ◽  
Acid Oxidase ◽  
Mechanistic Studies

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
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