scholarly journals Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria

1966 ◽  
Vol 241 (9) ◽  
pp. 2075-2083 ◽  
Author(s):  
Minoru Nakano ◽  
T.S. Danowski
1986 ◽  
Vol 34 (12) ◽  
pp. 1709-1718 ◽  
Author(s):  
N Usuda ◽  
S Yokota ◽  
T Hashimoto ◽  
T Nagata

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.


Author(s):  
Taizo Sasamura ◽  
Akihiko Matsuda ◽  
Yukifumi Kokuba

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.


1987 ◽  
Vol 19 (3) ◽  
pp. 157-169 ◽  
Author(s):  
M. E. Perotti ◽  
E. Gavazzi ◽  
L. Trussardo ◽  
N. Malgaretti ◽  
B. Curti

1979 ◽  
Vol 27 (3) ◽  
pp. 751-755 ◽  
Author(s):  
A W Chan ◽  
S G Perry ◽  
H B Burch ◽  
S Fagioli ◽  
T R Alvey ◽  
...  

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.


Author(s):  
Michiko Sukenobu Huynh ◽  
Kihachiro Horiike ◽  
Hiromasa Tojo ◽  
Masanao Katagiri ◽  
Toshio Yamano

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