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一种来自猴腮腺的异质性β-D-葡萄糖苷酶激活剂及其作为亲和配体在人唾液β-D-葡萄糖苷酶纯化中的应用。

A heterogeneous beta-D-glucosidase activator from monkey parotid gland and its use as an affinity ligand in the purification of human salivary beta-D-glucosidase.

作者信息

Nagarajan S, Cherian R, Balasubramanian A S

出版信息

Biochem Int. 1987 Feb;14(2):365-73.

PMID:3107568
Abstract

We have isolated a heat-stable, low molecular weight activator peptide(s) from monkey parotid gland that specifically activated human salivary beta-D-glucosidase. This activator appeared to be heterogeneous on Sephadex G-25 gel filtration and polyacrylamide gel electrophoresis under non-denaturing conditions. About 45% of the human salivary beta-glucosidase could bind to the activator immobilised on Sepharose and be eluted by Cutscum. The purified enzyme was nearly homogeneous, with a subunit Mr of 46,000 as revealed by SDS-gel electrophoresis and silver staining.

摘要

我们从猴腮腺中分离出一种热稳定的低分子量激活肽,它能特异性激活人唾液β-D-葡萄糖苷酶。在非变性条件下,这种激活剂在Sephadex G-25凝胶过滤和聚丙烯酰胺凝胶电泳中似乎具有异质性。约45%的人唾液β-葡萄糖苷酶能与固定在琼脂糖上的激活剂结合,并被Cutscum洗脱。经SDS-凝胶电泳和银染显示,纯化后的酶几乎是均一的,亚基分子量为46,000。

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