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인체 유방암에서 p16<SUP>INK4A</SUP> 단백 이상발현에 관한 면역조직화학적 분석
송태진(Tae Jin Song),문정석(Jeong Seok Moon),이은숙(Eun Suk Lee),이재복(Jae Bok Lee),최원준(Won Jun Choi),채기봉(Gi Bong Chae),목영재(Young Jae Mok),배정원(Jeoung Won Bae),원남희(Nam Hee Won),구범환(Bum Hwan Koo) 대한외과학회 1999 Annals of Surgical Treatment and Research(ASRT) Vol.56 No.3
박명근,Chang-Hao Cui,Sung Chul Park,박슬기,김진광,Mi-Sun Jung,정석채,김선창,임완택 한국미생물학회 2014 The journal of microbiology Vol.52 No.5
The focus of this study was the cloning, expression, andcharacterization of recombinant ginsenoside hydrolyzingβ-glucosidase from Arthrobacter chlorophenolicus with anultimate objective to more efficiently bio-transform ginsenosides. The gene bglAch, consisting of 1,260 bp (419 aminoacid residues) was cloned and the recombinant enzyme, overexpressedin Escherichia coli BL21 (DE3), was characterized. The GST-fused BglAch was purified using GST·Bind agaroseresin and characterized. Under optimal conditions (pH 6.0and 37°C) BglAch hydrolyzed the outer glucose and arabinopyranosemoieties of ginsenosides Rb1 and Rb2 at the C20position of the aglycone into ginsenoside Rd. This was followedby hydrolysis into F2 of the outer glucose moiety ofginsenoside Rd at the C3 position of the aglycone. Additionally,BglAch more slowly transformed Rc to F2 via C-Mc1(compared to hydrolysis of Rb1 or Rb2). These results indicatethat the recombinant BglAch could be useful for theproduction of ginsenoside F2 for use in the pharmaceuticaland cosmetic industries.