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
Hauptverfasser: YAGI, Toshiharu, MISONO, Haruo, KURIHARA, Norio, YAMAMOTO, Tatsuo, SODA, Kenji
Format: Artikel
Sprache:eng
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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.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a132880