Conversion of lysine to saccharopine by human tissues
| Autor: | Joseph Dancis, Joel Hutzler |
|---|---|
| Rok vydání: | 1968 |
| Předmět: |
Electrophoresis
Ammonium sulfate Lysine Biophysics Biology Reductase Kidney complex mixtures Biochemistry Glutarates chemistry.chemical_compound Oxidoreductase Humans Molecular Biology chemistry.chemical_classification Carbon Isotopes Sulfates Saccharopine dehydrogenase Dipeptides Hydrogen-Ion Concentration Chromatography Ion Exchange In vitro Cold Temperature Quaternary Ammonium Compounds Enzyme Liver chemistry Saccharopine Ketoglutaric Acids bacteria Oxidoreductases NADP |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 158:62-69 |
| ISSN: | 0304-4165 |
| Popis: | The ability of human tissues to convert lysine and α-ketoglutarate to saccharopine [ e-N-( l -glutaryl -2)- l -lysine ] has been investigated vitro. Liver is the most effective organ, though some activity could be demonstrated in several other tissues. The responsible enzyme lysine-ketoglutarate reductase (lysine:α-ketoglutarate: TPNH oxidoreductase ( e-N-[ glutaryl -2]- l -lysine forming )) has been partially purified from human liver and optimal conditions for its assay determined. There is a specific requirement for TPNH that cannot be satisfied by DPNH. A pH optimum near neutrality and inhibition by ammonium sulfate were observed. The enzyme is stable at −25°, both in tissues obtained at post-mortem and in its purified form. The assay for lysine-ketoglutarate reductase is sufficiently sensitive to be used on the limited amount of tissue obtainable by needle biopsy of the liver. |
| Databáze: | OpenAIRE |
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