scholarly journals Tissue fractionation studies. 17. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, alanine aminotransferase, d-amino acid oxidase and catalase in rat-liver tissue

1964 ◽  
Vol 92 (1) ◽  
pp. 179-184 ◽  
Author(s):  
P Baudhuin ◽  
H Beaufay ◽  
Y Rahman-Li ◽  
OZ Sellinger ◽  
R Wattiaux ◽  
...  
Keyword(s):  
Amino Acid ◽  
Monoamine Oxidase ◽  
Rat Liver ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Liver Tissue ◽  
Intracellular Distribution ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Tissue Fractionation

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.

scholarly journals Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue*

1955 ◽  
Vol 60 (4) ◽  
pp. 604-617 ◽  
Author(s):  
C. de Duve ◽  
B. C. Pressman ◽  
R. Gianetto ◽  
R. Wattiaux ◽  
F. Appelmans
Keyword(s):  
Rat Liver ◽  
Liver Tissue ◽  
Distribution Patterns ◽  
Intracellular Distribution ◽  
Tissue Fractionation

A quantitative histochemical study of D-amino acid oxidase activity in rat liver in relationship with feeding conditions.

1991 ◽  
Vol 39 (1) ◽  
pp. 81-86 ◽  
Author(s):  
H R Patel ◽  
W M Frederiks ◽  
F Marx ◽  
A J Best ◽  
C J Van Noorden
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Specific Inhibitor ◽  
Physiological Role ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Specific Test ◽  
Final Reaction Product ◽  
Final Reaction

The histochemical method for the demonstration of D-amino acid oxidase activity in rat liver, based on the use of cerium ions and the diaminobenzidine-cobalt-hydrogen peroxide procedure, was improved by the application of unfixed cryostat sections and a semipermeable membrane interposed between section and gelled incubation medium. The amount of final reaction product precipitated in a granular form was about four times higher with this technique in comparison with conventional procedures using fixed sections and aqueous incubation media. The specificity of the reaction was proven by the 70% reduction of the amount of final reaction product when incubating in the presence of substrate and D,L-beta-hydroxybutyrate, a specific inhibitor of D-amino acid oxidase activity. Cytophotometric analysis of liver sections revealed that the specific test minus control reaction was linear with incubation time and section thickness. The Km value of the enzyme of 10.3 +/- 2.7 mM, as determined in periportal areas, is about five times the value found with biochemical methods in liver cell homogenates. The enzyme activity in periportal areas is about five times the activity in pericentral areas. Fasting (24 and 48 hr) induced a significant decrease in D-amino acid activity in periportal and pericentral areas. The possible physiological role of the enzyme in liver is discussed.

Heterogenous staining ofd-amino acid oxidase in peroxisomes of rat liver and kidney

1988 ◽  
Vol 88 (3-6) ◽  
pp. 277-285 ◽  
Author(s):  
S. Angermüller ◽  
H. D. Fahimi
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Liver And Kidney

scholarly journals Immunoelectron microscopic study of a new D-amino acid oxidase-immunoreactive subcompartment in rat liver peroxisomes.

1991 ◽  
Vol 39 (1) ◽  
pp. 95-102 ◽  
Author(s):  
N Usuda ◽  
S Yokota ◽  
R Ichikawa ◽  
T Hashimoto ◽  
T Nagata
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Small Area ◽  
Electron Microscopic Observation ◽  
Glycolate Oxidase ◽  
Acid Oxidase ◽  
Electron Microscopic ◽  
Amino Acid Oxidase ◽  
The Matrix ◽  
Electron Lucent

We report the presence of a new subcompartment in rat liver peroxisomal matrix in which only D-amino acid oxidase is localized and other matrix enzymes are absent. By electron microscopic observation, the rat liver peroxisome has generally been considered to consist of a single limiting membrane, an electron-dense crystalline core, and a homogeneous matrix. Immunohistochemical staining for D-amino acid oxidase by the protein A-gold technique revealed the presence of a small area in the matrix that was immunoreactive for the enzyme and was less electron-dense than the surrounding matrix. The localization of D-amino acid oxidase in this small area of the peroxisomal matrix was confirmed by immunoelectron microscopy on freeze-substituted tissues processed without chemical fixation. To analyze the characteristics of the electron-lucent area, immunoreactivity for various peroxisomal enzymes, including catalase, acyl-CoA oxidase, enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein, 3-ketoacyl-CoA thiolase, L-alpha-hydroxy acid oxidase (isozyme B), and glycolate oxidase (isozyme A), was assayed. The electron-lucent area was negative for all of these. By double staining for D-amino acid oxidase and catalase, using colloidal gold particles of different sizes, these enzymes were shown to be located in separate areas in the matrix.

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.

Sign in / Sign up

Export Citation Format

Share Document