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방선균 분리주가 생산하는 Phospholipase C 저해물질인 MT2617-2B의 분리 및 특성
고학룡,이현선,오원근,안순철,김보연,강대욱,민태익,안종석 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.1
방선균 분리주 MT2617-2의 배양액으로 부터 phospholipase C (PLC) 저해물질인 MT2617-2B를 n-butanol 추출 및 column chromatography 법을 이용하여 분리하였다. MT2617-2B는 IR ^13C- 및 ^1H-NMR 그리고 ESI-MS에 의한 구조분석 결과, 한 개의 hemiketal ring, polyhydroxyl 및polymethyl groups으로 구성되었으며 side chain으로 한 개씩의 malonate 및 guanidine group을 가지는 분자량 1057의 macrolide 화합물이었다. 따라서, MT2617-2B를 기존의 macrolide 항생제인 copiamycin 및 niphithricin A로 동정하였다. 한편, MT2617-2B는 methanol 용액에서 실온에서 방치하였을 때 도일한 분자량을 가진 두 개의 이성질체를 생성하였다. PLC γ1과 -β1에 대해 각각 25 및 50㎍/㎖의 IC_50 값을 가지며, Staphylococcus aureus 와 Candida albicans에 대해서는 항균활성을 나타내지만 Escherichia coli에는 나타내지 않았다. A phospholipase C (PLC) inhibitor (MT2617-2B) was isolated from the culture broth of actionmycetes isolate MT2617-2 by the extraction with n-butanol and column chromatographic techniques. The molecular weight of the inhibitor was 1057, by the spectroscopic analyses of IR ^13C- and ^1H-NMR and ESI-MS. The chemical structure of MT2617-2B was found to be a macrolide compound consisted of a hemiketal ring, polyhydroxyl and polymethyl groups, which had a malonate and guanidine group as its side chain. MT2617-2B produced its two isomers having the same molecular weight by standing in methanol solution at room temperature. Therefore, MT2617-2B was identified as copiamycin and niphithricin A, macrolide antibiotics. The values of IC_50 against PLC γ1 and PLC-β1 were 25 and 50㎍/㎖, respectively. MT2617-2B had antimicrobial activities against Staphylococcus aureus and Candida albicans, but not against Escherichia coli.
김치유래 젖산균의 균체지방산 분석을 이용한 분류학적 연구
이정숙,정민철,김우식,이근철,김홍중,박찬선,이헌주,주윤정,이근종,안종석,박완,박용하,민태익 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.2
표준균주를 포함한 230여개의 김치유래 젖산균에 대한 균체지방산(FAMEs)을 분석하였다. FAMEs profiles는 Euclidian Distance 17.5에 의해 7개의 Major Cluster와 1개의 Single Cluster로 나뉘어졌다. 이중 A, B, C 및 Cluster는 Leuconostoc속으로 분석되어졌고, F는 Lactobacillus속으로 분석되어졌다. 그리고 E와 G cluster는 두개의 Genus가 혼재되어 나타났으며 보충적인 연구가 필요하다. 앞으로 김치유래 젖산균의 균체지방산 분석결과를 기반으로 한 데이타베이스에 95가지 탄소원을 이용하는 수치분류학적 접근방법 및 Pyrolysis Mass Spectrometry 등의 화학적 분석 방법과 분자친화적 연구를 통한 종합적 분류정보 체계가 갖추어지면 젖산균의 신속, 정확한 동정 및 연구에 활발히 이용되어질 것이다. Two hundreds and thirty lactic acid bacteria, mostly isolated from Kimchi, including type strains were sued for analysis of cellular fatty acids. The 230 test strains were recoverd in 7 major and 1 single clusters defined a Euclidian distance of 17.5. These aggregate taxa were equivalent to the genus Leuconostoc (aggregate group A, B, C and D), and the genera Leuconostoc and Lactobacillus (aggregate group G). It is concluded as evident that FAMEs (Fatty Acid Methyl Esters) profile of cell can be used as a criterion in classification of lactic acid bacterial from kimchi. Additional comparative taxonomic studies need to be carried out on well chosen representative strains to determine the most appropriate methods of value.
Chaetoglobosin A, an Inhibitor of Bleb Formation on K562 Cells Induced by Phorbol 12,13-Dibutyrate
KO, HACK-RYONG,KIM, BO YEON,AHN, SOON-CHEOL,OH, WON KEUN,KIM, JIN-HEE,LEE, HYUN SUN,KIM, HWAN-MOOK,HAN, SANG-BAE,MHEEN, TAE0ICK,AHN, JONG-SEOG 한국미생물 · 생명공학회 1998 Journal of microbiology and biotechnology Vol.8 No.6
Mheen, Tae Ick,Han, Moon H.,Seong, Baik Lin,Son, Hyeung Jin 생화학분자생물학회 1989 BMB Reports Vol.15 No.4
It was found that enzyme from a microbial strain, Monocillium sp. ATCC 20621 catalyzed the oxidative reaction of rifamycin B to form rifamycin O. The identification of the reaction products suggested that the reaction proceeded by the oxidative cyclization of rifamycin B to form rifamcycin O, which spontaneously hydrolyzed to rifamycin S in neutral aqueous milieu. The characteristics of enzyme was different as compared with that of other polyphenol oxidases such as lactase. It is proposed that this new type of enzyme be classified into subgroup EC 1. 10. 3. 6. with a trivial name rifamycin B oxidase.
Mheen, Tae Ick,Han, Moon H.,Seong, Baik L.,Park, Jong M.,Son, Hyeong J. 생화학분자생물학회 1989 BMB Reports Vol.15 No.4
Four kinds of enzyme preparations from Humicola sp. ATCC 20621 were used in this experiment, i.e., whole cell, defatted acetone dried powder, ammonium sulfate precipitate, and immobilized enzyme (defatted acetone dried powder entrapped in polyarylamide). The present enzyme was most specific for rifamycin B among various rifamycin derivatives and other similar golyol compounds. The Km values of soluble and immobilized enzyme for rifamycin B were 0.05 mM and 0.67 mM, respectively. The optimal pHs of soluble and immobilized enzyme for catalytic efficiency were 7.8 and 7.6, respectively, and the optimal temperatures were same in both of the enzymes. The enzyme activities were measured by two kinds of methods, dissolved oxygen consumption and spectrophotometric assay.