scholarly journals A purified cysteine conjugate beta-lyase from rat kidney cytosol. Requirement for an alpha-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K.

1986 ◽  
Vol 261 (33) ◽  
pp. 15529-15537 ◽  
Author(s):  
J L Stevens ◽  
J D Robbins ◽  
R A Byrd
Keyword(s):  
Amino Acid ◽  
Rat Kidney ◽  
Acid Oxidase ◽  
Keto Acid ◽  
Amino Acid Oxidase ◽  
Rat Kidney Cytosol

scholarly journals Immunocytochemical localization of D-amino acid oxidase in the central clear matrix of rat kidney peroxisomes.

1986 ◽  
Vol 34 (12) ◽  
pp. 1709-1718 ◽  
Author(s):  
N Usuda ◽  
S Yokota ◽  
T Hashimoto ◽  
T Nagata
Keyword(s):  
Amino Acid ◽  
Proximal Tubule ◽  
Rat Kidney ◽  
Protein A ◽  
Immunoblot Analysis ◽  
Acid Oxidase ◽  
Electron Microscopic ◽  
Amino Acid Oxidase ◽  
Thin Sections ◽  
Gold Particles

Light and electron microscopic localizations of D-amino acid oxidase (DAO) in rat kidney was investigated using immunoenzyme and protein A-gold techniques. The enzyme was purified from rat kidney homogenate and its antibody was raised in rabbits. By Ouchterlony double-diffusion analysis and immunoblot analysis with anti-(rat kidney DAO) immunoglobulin, the antibody was confirmed to be monospecific. The tissue sections (200 micron thick) of fixed rat kidney were embedded in Epon or Lowicryl K4M. Semi-thin sections were stained for DAO by the immunoenzyme technique after removal of epoxy resin for LM, and ultra-thin sections of Lowicryl-embedded material were labeled for DAO by the protein A-gold technique for EM. By LM, fine cytoplasmic granules of proximal tubule were stained exclusively. Among three segments of proximal tubules, and S2 and S3 segments were heavily stained but the S1 segment only weakly so. By EM, gold particles indicating the antigenic sites for DAO were exclusively confined to peroxisomes. Within peroxisomes, the gold particles were localized in the central clear matrix but not in the peripheral tubular substructures. The results indicate that D-amino acid oxidase in rat kidney is present exclusively in peroxisomes in the proximal tubule and that within peroxisomes it is found only in central clear matrix and not in the peripheral tubular substructures.

On the Reaction of ᴅ-Amino Acid Oxidase with β-Chloroalanine

1972 ◽  
Vol 27 (11) ◽  
pp. 1376-1378 ◽  
Author(s):  
Yoshihiro Miyake ◽  
Teruko Abe ◽  
Toshio Yamano
Keyword(s):  
Oxygen Consumption ◽  
Amino Acid ◽  
Slow Phase ◽  
Acid Oxidase ◽  
Keto Acid ◽  
Amino Acid Oxidase ◽  
Oxidation Reduction ◽  
Rapid Formation ◽  
Reaction Proceeds ◽  
Anaerobic Reaction

The reactions of ᴅ-amino acid oxidase with β-chloro-ᴅ-alanine and β-chloro-ʟ-alanine have been described. Both the holoenzyme and the apoenzyme catalyse the deamination of β-chloro-ʟ-alanine to keto acid without any consumption of oxygen or oxidation-reduction of the enzyme-bound FAD. The anaerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine involves three phases with respect to the reduction of the enzyme-bound FAD, the rapid formation of an intermediate spectral species followed by a steady state of this intermediate and the last decay of the intermediate to the fully reduced enzyme. The rate of keto acid formation decreases as the reaction proceeds and ceases at the beginning of the conversion of the intermediate to the fully reduced enzyme. The aerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine is biphasic. The first rapid oxygen consumption is followed by the second slow oxygen consumption. The second slow phase disappears by treating the enzyme with glutathione before the addition of substrate.

scholarly journals Determination of D-Amino Acid Oxidase Activity in Tumour Cells

2002 ◽  
Vol 39 (6) ◽  
pp. 595-598 ◽  
Author(s):  
Taizo Sasamura ◽  
Akihiko Matsuda ◽  
Yukifumi Kokuba
Keyword(s):  
Amino Acid ◽  
Cancer Patients ◽  
Rat Liver ◽  
Rat Kidney ◽  
Tumour Cells ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Tissue Samples ◽  
Host Tissues

Background We evaluated the assay for determining D-amino acid oxidase (DAAO) activity in tumour cells, rat liver and rat kidney for studying the effects of D-amino acid-containing solution on cancer patients. Methods and Results In this method the amount of ammonia produced by the DAAO activity after removal of endogenous ammonia using a Sephadex G25 column was determined. The highest activity was observed in rat kidney, which was almost eight times that found in rat liver. As compared with host tissues, the DAAO activity in tumour cells was considerably less. Conclusions This DAAO assay may be useful for analysis of various tissue samples as well as tumour cells.

Immunoelectron microscopic localization ofd-amino acid oxidase in rat kidney and liver

1987 ◽  
Vol 19 (3) ◽  
pp. 157-169 ◽  
Author(s):  
M. E. Perotti ◽  
E. Gavazzi ◽  
L. Trussardo ◽  
N. Malgaretti ◽  
B. Curti
Keyword(s):  
Amino Acid ◽  
Rat Kidney ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Microscopic Localization

scholarly journals Distribution of two aminotransferases and D-amino acid oxidase within the nephron of young and adult rats.

1979 ◽  
Vol 27 (3) ◽  
pp. 751-755 ◽  
Author(s):  
A W Chan ◽  
S G Perry ◽  
H B Burch ◽  
S Fagioli ◽  
T R Alvey ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Rat Kidney ◽  
Mirror Image ◽  
Acid Oxidase ◽  
Straight Segment ◽  
Amino Acid Oxidase ◽  
Adult Rats ◽  
Thin Limb

In the adult rat kidney, alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1) and D-amino acid oxidase (EC 1.4.3.3) were measured in glomeruli, 4 parts of the proximal tubule, 2 parts of the distal tubule and in patches from the thin limb area and the papilla. These enzymes were measured in more limited parts of the nephron during postnatal development. Adult aspartate aminotransferase activities (percentage of the highest) ranged from 100 in the distal straight segment to 25 in the late part of the proximal straight segment to 10 in the thin limb and papillary area. Alanine aminotransferase (lower by a factor of 100 in absolute terms) was distributed as the mirror image of aspartate aminotransferase within proximal and distal tubules. D-Amino acid oxidase was 850-fold higher in proximal straight segments than in medullary structures. During development alanine aminotransferase increased 6-fold and D-amino acid oxidase, 4.5-fold in proximal straight tubules but aspartate aminotransferase increased in distal straight tubles 8-fold.

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