猪甲状腺聚焦酶

Deborah Shuey Grove , George S. Serif
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引用次数: 17

摘要

从猪甲状腺组织中分离到一种α-l- focusidase (α-l- focuside岩藻水解酶,EC 3.2.1.51),采用离子交换、亲和和分子筛色谱相结合的方法对其进行了10 800倍的纯化。SDS电泳显示酶是均匀的,但等电聚焦程序检测到相当大的异质性。酶是一种糖蛋白,这一事实干扰了SDS电泳或分子筛技术准确的分子量估计。然而,该酶似乎是一个四聚体,密度梯度测量将其分子量设定为19200±3000。该酶在pH为5.1时表现出最佳,并对通过α键连接的l-聚焦单元表现出高度的特异性。巯基和羧基似乎都是酶活性所必需的。这种酶不会直接攻击完整的甲状腺球蛋白,但如果蛋白质部分被大量去除,它会去除糖基部分的聚焦基残基。因此,当甲状腺球蛋白被降解时,这种酶起着挽救作用。
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Porcine thyroid fucosidase

An α-l-fucosidase (α-l-fucoside fucohydrolase, EC 3.2.1.51) has been isolated from porcine thyroid tissue and purified 10 800-fold using a combination of ion exchange, affinity and molecular sieve chromatography. The enzyme appears homogeneous by SDS electrophoresis but isoelectric focusing procedures detect considerable heterogeneity. The enzyme is a glycoprotein and this fact interferes with accurate molecular weight estimates by SDS electrophoresis or molecular sieve techniques. The enzyme appears, however, to be a tetramer and density gradient measurements set its molecular weight at 19200 ± 3000. The enzyme exhibits an optimum at a pH of 5.1 and shows a high order of specificity for l-fucose units linked through α bonds. Both sulfhydryl and carboxyl groups appear necessary for enzyme activity. The enzyme does not attack intact thyroglobulin directly but will remove fucosyl residues from the glycome moiety if the protein portion is largely removed. The enzyme thus functions in a salvage role as thyroglobulin is degraded.

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