变形链球菌c血清型细胞外D-葡萄糖基转移酶的纯化与特性分析
Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.
作者信息
Baba T, Ogawa T, Okahashi N, Yakushiji T, Koga T, Morimoto M, Hamada S
出版信息
Carbohydr Res. 1986 Dec 15;158:147-55. doi: 10.1016/0008-6215(86)84013-7.
A simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans.
利用DEAE-葡聚糖凝胶和CM-纤维素柱色谱法，开发了一种从变形链球菌血清型c菌株中纯化细胞外D-葡萄糖基转移酶（GTase）的简单方法。该GTase分子量为155,000，等电点为7.4。在没有右旋糖酐T-10的情况下，该酶将蔗糖转化为具有一些α-(1→3)-连接的D-葡萄糖基残基的分支(1→6)-连接的α-D-葡聚糖。该GTase与从血清型c变形链球菌的其他菌株中分离出来并合成水溶性葡聚糖的GTase相似。此外，该GTase蛋白的氨基酸组成与合成水溶性和水不溶性葡聚糖的血清型g变形链球菌的GTase相对相似。
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