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Serratia marcescens 로 부터 5 가지 Chitinase Isozymes 의 동정
황재령,갈상완,이경애,신용철,조무제,이상열 ( Jae Ryoung Hwang,Sang Wan Gal,Kyeong Ai Lee,Yong Chul Shin,Moo Je Cho,Sang Yeol Lee ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.3
S. marcescens KCTC2172 produced five extracellular chitinases that were involved in chitin degradation. These enzymes were identified as chitinase isozymes by substrate activity staining in SDS-PAGE gel after removal of SDS, because chitinases were resistant to SDS and existed as monomeric proteins. Their apparent molecular weights obtained by SDS-PAGE were 58, 47, 43, 37, and 21 kd. The chitinase activities were induced about seven folds by the addition of 1.5% chitin to LB-medium compared with those obtained without chitin, and the induction was dependent on the various forms of chitin. Chitinases were purified using the regenerated chitin column by successive pH changes of elution buffer. When the column was eluted with enough volume of pH 3.3 buffer, five chitinase isozymes were eluted. However, three of them whose molecular weights were 58, 47 and 43 kd were further eluted by the pH changes of elution buffer from pH 3.3 to 2.0. Considering the pH dependent stability of chitinases, it was known that S. marcescens produced two groups of chitinase isozymes; One is resistant and the other is very sensitive to acidic conditions, at pH below 3.3.
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Identification of Five Chitinase Isozymes from S. marcescens
Hwang, Jae Ryoung,Gal, Sang Wan,Lee, Kyeong Ai,Shin, Yong Chul,Cho, Moo Je,Lee, Sang Yeol 慶尙大學校 기초과학연구소 1991 基礎科學硏究所報 Vol.7 No.-
SDS 존재하에서 전기영동을 한 후, substrate activity staining을 한 결과, S. marcescens는 5가지의 chitinase isozyme을 생성함을 알아내었다. 이 효소는 inducible enzyme으로서, 30℃에서 7일간 진탕배양하였을 때 1.5% chitin을 첨가한 LB-배지에서 얻은 효소활성이 chitin을 첨가하지 않은 배지에서 얻은 것보다 약 7배의 효소활성의 증가를 보였다. Chitinase를 최대로 생성시키는 조건에서 S. marcescens를 배양한 후 regenerated chitin을 이용한 친화성 chromatography를 행하여, 이 배양상등액으로부터 5가지의 chitinase isozyme를 분리하였으며 이들의 분자량이 58, 47, 43, 37 및 21 kd임을 확인하였다. 충분히 세척한 chitin column으로부터 chitinase를 elution시키는 방법으로, pH3.3인 완충액을 사용하였을 때, 5가지 chitinases가 모두 용출되었으며, pH를 2.0인 완충액으로 바꾸어 용출시켰더니 5가지 중 분자량이 58, 47, 43 kd인 3가지 chitinase가 더 회수되었다. 또한 Chitinases 의 pH에 대한 안정성을 실험한 결과 S. marcescens가 분비하는 chitinases는 산성조건에서 매우 불안전한 chitinases와 비교적 안정한 chitinase의 두가지 group이 존재함을 알 수 있었다. S. marcescescens KCTC2172 produced five extracellular chitinases that were involved in chitin degradation. These enzymes were identified as chitinase isozymes by substrate activity staining in SDS-PAGE gel after removal of SDS, because chitinases were resistant to SDS and existed as monomeric proteins. Their apparent molecular weights obtained by SDS-PAGE were 58, 47, 43, 37, and 21kd. The chitinase activities were induced about seven folds by the addition of 1.5% chitin to LB-medium compared with those obtained without chitin, and the induction was dependent on the various forms of chitin. Chitinases were purified using the regenerated chitin column by successive pH changes of elution buffer. When the column was eluted with enough volume of pH 3.3 buffer, five chitinase isozymes were eluted. However, three of them whose molecular weights were 58,47 and 43 kd were further eluted by the pH changes of elution buffer from pH 3.3 to 2.0 Considering the pH dependent stability of chitinases, it was known that S. marcescens produced two groups of chitinase isozymes; One is resistant and the other is very sensitive to acidic conditions, at pH below 3.3.
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Antifungal Activity of Serratia marcescens Chitinases against Phytopathogenic Fungi
CHO, MOO JE,GAL, SANG WAN,HWANG, JAE RYOUNG,SHIN, YONG CHUL,LEE, SANG YEOL 경상대학교 유전공학연구소 1990 遺傳工學硏究所報 Vol.9 No.-
The extracellular chitinase activities of Serratia marcescens were induced by the addition of 1.5% swollen chitin to LB-broth about seven folds compared to that obtained from the culture medium without chitin. S. marcescens was co-cultured with various phytopathogenic fungi, including Phytophtora parasitica, Botryosphaeria oxyaporium in an LB-agar medium containing 1.5% swollen chitin. Fungal hyphae grew rapidly outward from the center, however the hyphal extension of pathogenic fungi was significantly inhibited in a perimetric contract area with S. marcescens. Each of the culture supernatant of S. marcescens, E. coli, or the chitinase of Streptomyces griceus purchased from Sigma was incubated with the mycelium of F. oxysporium as a sole carbon source in a slide glass with single depressiom under the inverted microscope at 30℃. It was observed that the mycelium of F. oxysporium was gradually bursted as the cultivation time increased and completely lysed after incubation for 24 hrs by the chitinolytic activities of S. marcescens. From these data, it was concluded that the chitinolytic activites of S. marcescens play an important role in biocontrol of phytopathogenic fungi.
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Interaction between IGFBP-5 and TNFR1
Eun Jung Kim,정미숙,황재령,Je-Ho Lee,장세복 대한화학회 2010 Bulletin of the Korean Chemical Society Vol.31 No.7
Insulin-like growth factor binding protein 5 (IGFBP-5) plays an important role in controlling cell survival, differentiation and apoptosis. Apoptosis can be induced by an extrinsic pathway involving the ligand-mediated activation of death receptors such as tumor necrosis factor receptor 1 (TNFR1). To determine whether IGFBP-5 and TNFR1 interact as members of the same apoptosis pathway, recombinant IGFBP-5 and TNFR1 were isolated. The expression and purification of the full-length TNFR1 and truncated IGFBP-5 proteins were successfully performed in E. coli. The binding of both IGFBP-5 and TNFR1 proteins was detected by surface plasmon resonance spectroscopy (BIAcore),fluorescence measurement, electron microscopy, and size-exclusion column (SEC) chromatography. IGFBP-5 indeed binds to TNFR1 with an apparent KD of 9 nM. After measuring the fluorescence emission spectra of purified IGFBP-5and TNFR1, it was found that the tight interaction of these proteins is accompanied by significant conformational changes of one or both. These results indicate that IGFBP-5 acts potently as a novel ligand for TNFR1.
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