STEROID-1-DEHYDROGENASE OF RHODOCOCCUS-ERYTHROPOLIS - PURIFICATION AND N-TERMINAL AMINO-ACID-SEQUENCE

被引：16

作者：

KAUFMANN, G

THOLE, H

KRAFT, R

ATRAT, P

机构：

[1] INST MICROBIOL & EXPTL THERAPY,O-6900 JENA,GERMANY

[2] MAX PLANCK INST EXPTL ENDOCRINOL,W-3000 HANNOVER,GERMANY

[3] CENT INST MOLEC BIOL,O-1115 BERLIN,GERMANY

来源：

JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1992年 / 43卷 / 04期

关键词：

D O I：

10.1016/0960-0760(92)90164-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：297 / 301

页数：5

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