Purification and properties of 4-aminobutyrate 2-ketoglutarate aminotransferase from pig liver
| Autor: | Pierre Gonnard, Marcienne Bloch-Tardy, Anne M. Buzenet, Christiane Fages |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
chemistry.chemical_classification
Metabolic function Chromatography Macromolecular Substances Swine 2-Ketoglutarate Aminobutyrate Cationic polymerization General Medicine Biology Hydrogen-Ion Concentration Molecular Weight Electrophoresis Kinetics Enzyme chemistry Biochemistry Liver Liver enzyme 4-Aminobutyrate Transaminase Animals Ketoglutaric Acids Pig liver Transaminases |
| Zdroj: | Biochimica et biophysica acta. 522(2) |
| ISSN: | 0006-3002 |
| Popis: | 4-Aminobutyrate-transaminase (4-aminobutyrate : 2-oxoglutarate aminotransferase, EC 2.6.1.19) from pig liver has been purified to electrophoretic homogeneity. It has a molecular weight of about 110 000 and is composed of two subunits of the same molecular weight but of different charges. Two forms of pig liver 4-aminobutyrate-transaminase were isolated by DEAE-cellulose chromatography and designated as 4-aminobutyrate-transaminase I and 4-aminobutyrate-transminase II, corresponding to a cationic and anionic form. Some physical and kinetic properties of liver enzyme were compared to those of brain enzyme and no significant differences were found, except for their sedimentation coefficients and the charges of their subunits. The role of 4-aminobutyrate-transaminase in liver remains a matter of speculation, but could be related to a metabolic function. |
| Databáze: | OpenAIRE |
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