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
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container_issue 4
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container_title The Journal of steroid biochemistry and molecular biology
container_volume 43
creator Kaufmann, Günter
Thole, Hubert
Kraft, Regine
Atrat, Peter
description 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.
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subjects 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
title Steroid-1-dehydrogenase of Rhodococcus erythropolis: Purification and N-terminal amino acid sequence
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