L-Lysine: 2-Oxoglutarate 6-Aminotransferase
L-Lysine:2-oxoglutarate 6-aminotransferase from Flavobacterium lutescence (=Achromobacter liquidum)2 has been shown to be composed of one each of four non-identical subunits, A, B1, B2, and C. The subunits were isolated by gel filtration, and DEAE-cellulose chromatography in the presence of 8 M urea...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 1980-04, Vol.87 (5), p.1395-1402 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | L-Lysine:2-oxoglutarate 6-aminotransferase from Flavobacterium lutescence (=Achromobacter liquidum)2 has been shown to be composed of one each of four non-identical subunits, A, B1, B2, and C. The subunits were isolated by gel filtration, and DEAE-cellulose chromatography in the presence of 8 M urea. Their molecular weights were determined by ultracentrifugation, gel electrophoresis and gel filtration: subunit A 24,000; B1 28,000; B2, 28,000; C 45,000. These subunits were all different in amino acid composition. Of the two molecules of bound pyridoxal 5′-phosphate, the one which absorbs at 415 nm is bound to subunit B2 and participates in the catalytic action of the enzyme. |
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ISSN: | 0021-924X 1756-2651 |
DOI: | 10.1093/oxfordjournals.jbchem.a132880 |