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用溴化氰裂解对晶状体纤维连接蛋白MP26进行结构研究。

Structural studies of lens fiber junction protein MP26 by cyanogen bromide cleavage.

作者信息

Alcala J, Lawniczak J, Putt D, Maisel H

机构信息

Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, Michigan 48201.

出版信息

Biochem Biophys Res Commun. 1987 Sep 30;147(3):1013-20. doi: 10.1016/s0006-291x(87)80171-7.

Abstract

The lens fiber-cell plasma membrane MP26 from chick, bovine, and human lenses yielded identical cyanogen bromide peptide maps, confirming the essential conservation of structure in the junction protein of vertebrate lens fiber cells. Immunoblot analyses of the cyanogen bromide peptide maps of human lens MP26 and of its age-dependent proteolytic product MP22 confirmed that MP22 is a derivative of MP26. The findings in this study are the first consistent with the positioning of the methionine residues in lens MP26 as predicted by its cDNA-derived sequence.

摘要

来自鸡、牛和人类晶状体的晶状体纤维细胞质膜MP26产生了相同的溴化氰肽图谱,证实了脊椎动物晶状体纤维细胞连接蛋白结构的基本保守性。对人类晶状体MP26及其年龄依赖性蛋白水解产物MP22的溴化氰肽图谱进行免疫印迹分析,证实MP22是MP26的衍生物。本研究中的发现首次与根据其cDNA衍生序列预测的晶状体MP26中甲硫氨酸残基的定位一致。

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Glycation of MP26 and MP22 in bovine lens membranes.
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