Jang I S, Kim D H
College of Pharmacy, Kyung-Hee University, Seoul, Korea.
Biol Pharm Bull. 1996 Dec;19(12):1546-9. doi: 10.1248/bpb.19.1546.
An alpha-L-rhamnosidase (EC 3.2.1.40) was purified 1500-fold from Bacteroides JY-6, an intestinal anaerobic bacterium of human. The specific activity of purified enzyme was 89.9 mumol/min/mg protein. The enzyme (M.W. 240000) is composed of two subunits of M.W. 120000 with pI and optimal pH values of 4.2 and 7.0, respectively. The apparent Kms for naringin, rutin and p-nitrophenyl-alpha-L-rhamnopyranoside were determined to be 0.89, 1.44 and 0.29 mM, respectively. The enzyme was strongly inhibited by L-rhamnose, L-fucose, saccharic acid 1,4-lactone, p-chlormercuriphenylsulfonic acid and Pb2+.
从人肠道厌氧菌拟杆菌JY-6中纯化出一种α-L-鼠李糖苷酶（EC 3.2.1.40），纯化倍数为1500倍。纯化酶的比活性为89.9 μmol/分钟/毫克蛋白。该酶（分子量240000）由两个分子量为120000的亚基组成，其pI和最适pH值分别为4.2和7.0。柚皮苷、芦丁和对硝基苯基-α-L-鼠李糖苷的表观Km值分别测定为0.89、1.44和0.29 mM。该酶受到L-鼠李糖、L-岩藻糖、糖二酸1,4-内酯、对氯汞基苯磺酸和Pb2+的强烈抑制。
