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酸性α-葡萄糖苷酶的前体作为一种膜结合酶被合成。

The precursor of acid alpha-glucosidase is synthesized as a membrane-bound enzyme.

作者信息

Tsuji A, Suzuki Y

机构信息

Division of Inherited Metabolic Disease, National Institute of Neuroscience, Tokyo, Japan.

出版信息

Biochem Int. 1987 Nov;15(5):945-52.

PMID:3325063
Abstract

A pulse-chase study in human skin fibroblasts showed that a 110 kDa precursor of acid alpha-glucosidase was synthesized as a membrane-bound protein, which was solubilized in vitro not by mannose 6-phosphate or 1M KCl but by Triton X-100 or trypsin. This 110 kDa precursor form bound to the membrane was detected in control fibroblasts treated with tunicamycin and in I-cell disease fibroblasts as well. The precursors in human placenta were found also in the membrane fraction. It was concluded that the newly synthesized acid alpha-glucosidase precursor is located on the surface of the membrane, and the phosphomannosyl receptor does not participate in the enzyme-membrane binding.

摘要

一项针对人类皮肤成纤维细胞的脉冲追踪研究表明,酸性α-葡萄糖苷酶的110 kDa前体作为一种膜结合蛋白被合成,在体外,它不被6-磷酸甘露糖或1M氯化钾溶解,而是被曲拉通X-100或胰蛋白酶溶解。在用衣霉素处理的对照成纤维细胞以及I-细胞病成纤维细胞中也检测到了这种与膜结合的110 kDa前体形式。人胎盘中的前体也存在于膜组分中。得出的结论是,新合成的酸性α-葡萄糖苷酶前体位于膜表面,磷酸甘露糖受体不参与酶与膜的结合。

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