鼠李糖乳杆菌甘油脱水酶的纯化和性质研究。
Purification and Characterization of Glycerol Dehydratase from Lactobacillus reuteri.
机构信息
Department of Microbiology, North Carolina State University, Raleigh, North Carolina 27695.
出版信息
Appl Environ Microbiol. 1990 Apr;56(4):1195-7. doi: 10.1128/aem.56.4.1195-1197.1990.
Abstract
A coenzyme B(12)-dependent glycerol dehydratase from Lactobacillus reuteri has been purified and characterized. The dehydratase has a molecular weight of approximately 200,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single major band with a molecular weight of 52,000. K(m) values for substrates and coenzyme B(12) were in the millimolar and the submicromolar range, respectively.
摘要
鼠李糖乳杆菌依赖辅酶 B(12)的甘油脱水酶已被纯化和鉴定。该脱水酶的分子量约为 200,000，十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示分子量为 52,000 的单一主要条带。底物和辅酶 B(12)的 K(m) 值分别在毫摩尔和亚毫摩尔范围内。
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