Steroid-1-dehydrogenase of Rhodococcus erythropolis: Purification and N-terminal amino acid sequence

The inducible steroid-1-dehydrogenase from the bacterium Rhodococcus erythropolis IMET 7030 was purified to homogeneity using affinity chromatographic, electrophoretic, and ion exchange techniques. The spectrum of the pure enzyme is characterized by the associated FAD. The M r of the enzyme is 56,00...

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Veröffentlicht in:	The Journal of steroid biochemistry and molecular biology 1992-10, Vol.43 (4), p.297-301
Hauptverfasser:	Kaufmann, Günter, Thole, Hubert, Kraft, Regine, Atrat, Peter
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biological and medical sciences Chromatography, High Pressure Liquid Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Molecular Sequence Data Oxidoreductases Oxidoreductases - chemistry Oxidoreductases - isolation & purification Oxidoreductases - metabolism purification Rhodococcus - enzymology Rhodococcus erythropolis steroid-1-dehydrogenase
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Beschreibung
Zusammenfassung:	The inducible steroid-1-dehydrogenase from the bacterium Rhodococcus erythropolis IMET 7030 was purified to homogeneity using affinity chromatographic, electrophoretic, and ion exchange techniques. The spectrum of the pure enzyme is characterized by the associated FAD. The M r of the enzyme is 56,000. The amino acid composition and the sequence of the 13 N-terminal amino acids are given.
ISSN:	0960-0760 1879-1220
DOI:	10.1016/0960-0760(92)90164-E