来自噬纤维菌属L43 - 1菌株的胶原酶的纯化及性质
Purification and properties of collagenase from Cytophaga sp. L43-1 strain.
作者信息
Sasagawa Y, Kamio Y, Matsubara Y, Matsubara Y, Suzuki K, Kojima H, Izaki K
机构信息
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
出版信息
Biosci Biotechnol Biochem. 1993 Nov;57(11):1894-8. doi: 10.1271/bbb.57.1894.
A collagenolytic bacterial strain was isolated from soil and was identified as Cytophaga sp. It produced several kinds of collagenase and protease. From the supernatant of a culture, a collagenase was purified as a single protein band upon SDS-PAGE and its molecular mass was estimated to be 120 kDa. Collagen and gelatin were good substrates for this enzyme. beta-Casein was cleaved by this enzyme at several sites.
从土壤中分离出一株胶原分解菌，鉴定为噬纤维菌属。它能产生多种胶原酶和蛋白酶。从培养物的上清液中，一种胶原酶经SDS-PAGE纯化后呈现为单一蛋白条带，其分子量估计为120 kDa。胶原蛋白和明胶是该酶的良好底物。β-酪蛋白在多个位点被该酶切割。
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