Peroxisomal and mitochondrial proliferation and increased alanine:glyoxylate aminotransferase activity in human liver after chlorpromazine-induced cholestasis

1989 ◽  
Vol 17 (6) ◽  
pp. 1071-1072 ◽  
Author(s):  
PENNY J. COOPER ◽  
CHRISTOPHER J. DANPURE ◽  
KENNETH J. SIMPSON
Keyword(s):  
Human Liver ◽  
Aminotransferase Activity ◽  
Alanine:Glyoxylate Aminotransferase

Re-Evaluation of Conditions Required for Measurement of True Alanine:Glyoxylate Aminotransferase Activity in Human Liver: Implications for the Diagnosis of Hyperoxaluria Type I

1994 ◽  
Vol 31 (4) ◽  
pp. 361-366 ◽  
Author(s):  
V Andy P Horváth ◽  
Ronald J A Wanders
Keyword(s):  
Human Liver ◽  
Reliable Method ◽  
Type I ◽  
Aminotransferase Activity ◽  
Hyperoxaluria Type I ◽  
Alanine:Glyoxylate Aminotransferase ◽  
Liver Homogenates ◽  
Higher Sensitivity ◽  
Hyperoxaluria Type

In this paper we studied the glyoxylate-dependent transamination of L-alanine and L-glutamate in human liver homogenates in order to develop a reliable method for the determination of true alanine:glyoxylate aminotransferase activity in liver homogenates from patients suspected to suffer from hyperoxaluria type I. Measurements were made according to two protocols described in literature in control human liver homogenates which were either untreated or treated with an antiserum raised against purified alanine:glyoxylate aminotransferase. The results obtained show that enzyme activity can best be determined at pH 8.0 as compared to pH 7.4 since the former leads to a higher sensitivity of the method. Alanine:glyoxylate aminotransferase activities measured at pH 8.0 are approximately 50% higher compared to the enzyme activities measured at pH 7.4. Accordingly, it is proposed to measure alanine:glyoxylate aminotransferase activity at pH 8.0 using the newly determined correction factor as described in this paper.

scholarly journals Assay of alanine:glyoxylate aminotransferase in human liver by its serine: glyoxylate aminotransferase activity

2009 ◽  
Vol 30 (5) ◽  
pp. 295-301 ◽  
Author(s):  
Masao Nagata ◽  
Arata Ichiyama ◽  
Tatsuya Takayama ◽  
Toshiaki Oda ◽  
Soichi Mugiya ◽  
...  
Keyword(s):  
Human Liver ◽  
Aminotransferase Activity ◽  
Alanine:Glyoxylate Aminotransferase ◽  
Glyoxylate Aminotransferase

scholarly journals Molecular Insight into the Synergism between the Minor Allele of Human Liver Peroxisomal Alanine:Glyoxylate Aminotransferase and the F152I Mutation

2009 ◽  
Vol 284 (13) ◽  
pp. 8349-8358 ◽  
Author(s):  
Barbara Cellini ◽  
Riccardo Montioli ◽  
Alessandro Paiardini ◽  
Antonio Lorenzetto ◽  
Carla Borri Voltattorni
Keyword(s):  
Human Liver ◽  
Minor Allele ◽  
Alanine:Glyoxylate Aminotransferase ◽  
Insight Into

Capillary electrophoresis assay of alanine:glyoxylate aminotransferase activity in rat liver

2002 ◽  
Vol 780 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Saori Nishijima ◽  
Kimio Sugaya ◽  
Makoto Morozumi ◽  
Tadashi Hatano ◽  
Yoshihide Ogawa
Keyword(s):  
Capillary Electrophoresis ◽  
Rat Liver ◽  
Aminotransferase Activity ◽  
Alanine:Glyoxylate Aminotransferase

Multiple Molecular Forms of Human Heart Cytoplasmic Aspartate Aminotransferase

1982 ◽  
Vol 62 (3) ◽  
pp. 337-339 ◽  
Author(s):  
F. Y. Leung ◽  
A. R. Henderson
Keyword(s):  
Isoelectric Focusing ◽  
Aspartate Aminotransferase ◽  
Human Liver ◽  
Human Heart ◽  
Specific Activity ◽  
Molecular Forms ◽  
Aminotransferase Activity ◽  
Multiple Molecular Forms ◽  
Isoelectric Points

1. Cytoplasmic aspartate aminotransferase was isolated and purified from human heart with a final specific activity of 236 units/mg of protein. 2. Three distinct peaks of aspartate aminotransferase activity were detected by isoelectric focusing with isoelectric points of 5.46, 5.60 and 5.71. Two minor subforms were also noted as shoulder patterns with pI 5.2 and 5.8. 3. These electrophoretic characteristics are similar to previous findings of multiple molecular forms detected in human liver and erythrocytes.

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