Mycobacterium fortuitum의 스테로이드 9alpha-하이드록실라제의 분리 및 부분정제

• 영문명: Isolation and Partial Purification of the Steroid 9alpha-Hydroxylase from Mycobacterium fortuitum
• 발행기관: 대한약학회
• 저자명: 강희경(Hee Kyoung Kang)
• 간행물 정보: 『약학회지』제41권 제5호 (1997년), 638~646쪽, 전체 9쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 1997.10.31

영문 초록

The steroid 9alpha-hydroxylase activity has been detected in cytosol fraction, 100,00OXg supernatant of cell free extract of Mycobacterium fortuitum. The activity was not linear viith protein concentration in the assay suggesting 9alpha-hydroxylase is a multicomponent enzyme. The 9alpha-hydroxylase system was partially purified through fractional saturation of ammonium sulfate, strong anion exchange (Mono Q) column chromatography, gel filtration (Superose 12) column chromatography, and testosterone affinity gel chromatography. Ammonium sulfate 50~60% saturated fraction of the cytosol gave 9alpha-hydroxylase activity. For further purification, the half-saturated ammonium sulfate fraction was applied to Mono Q, Superose 12, or affinity gel column. The purification factors of 9alpha-hydroxylase containing fraction after Mono Q, Superose 12, and affinity gel chromatography was 13, 11, and 17 respectively.

키워드

steroid 9α-hydroxylase partial purification multicomponent enzyme fractional saturation of ammonium sulfate Mono Q chromatography Superose 12 chromatography testosterone affinity gel chromatography.