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牛晶状体中类4.1带蛋白。分化、分布及提取特性的影响

Band 4.1-like proteins of the bovine lens. Effects of differentiation, distribution and extraction characteristics.

作者信息

Aster J C, Brewer G J, Hanash S M, Maisel H

出版信息

Biochem J. 1984 Dec 1;224(2):609-16. doi: 10.1042/bj2240609.

DOI:10.1042/bj2240609
PMID:6517866
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1144471/
Abstract

Bovine lens epithelium, cortex and nucleus were screened for the presence of red-cell-membrane band 4.1-like proteins by using an immunoblot method. Lens epithelial cells were found to contain proteins of Mr 78 000 and higher (approximately 150 000) that cross-reacted with anti-(protein 4.1) sera. Fibre cells of the superficial cortex were also found to contain these two proteins, as well as an additional protein of approx. 80 000 Mr. In contrast, deep layers of the cortex and the lens nucleus contained no detectable cross-reactive protein at these Mr values. Treatment of a crude membrane fraction prepared from superficial bovine cortices with a low-ionic-strength buffer resulted in release of the high-Mr band 4.1-like protein. The 80 000- and 78 000-Mr proteins remained with the membrane fraction in low-ionic-strength buffer, but were released into solution by high-ionic-strength-buffer treatment. We have also demonstrated that the human red-blood-cell membrane, like lens epithelial cells and fibre cells, also contains a high-Mr band 4.1-like protein that is released from membranes by low-ionic-strength-buffer treatment.

摘要

采用免疫印迹法对牛晶状体上皮、皮质和核进行筛选,以检测是否存在红细胞膜带4.1样蛋白。发现晶状体上皮细胞含有分子量为78000及以上(约150000)的蛋白,这些蛋白与抗(蛋白4.1)血清发生交叉反应。还发现表层皮质的纤维细胞含有这两种蛋白,以及另一种分子量约为80000的蛋白。相比之下,皮质深层和晶状体核在这些分子量值下未检测到交叉反应蛋白。用低离子强度缓冲液处理从牛表层皮质制备的粗膜组分,可使高分子量的带4.1样蛋白释放出来。分子量为80000和78000的蛋白在低离子强度缓冲液中仍留在膜组分中,但通过高离子强度缓冲液处理可释放到溶液中。我们还证明,人红细胞膜与晶状体上皮细胞和纤维细胞一样,也含有一种高分子量的带4.1样蛋白,该蛋白可通过低离子强度缓冲液处理从膜中释放出来。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/4230060ab88f/biochemj00314-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/1361a8963cb1/biochemj00314-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/1bced78c989a/biochemj00314-0269-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/d506e38c437f/biochemj00314-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/4230060ab88f/biochemj00314-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/1361a8963cb1/biochemj00314-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/1bced78c989a/biochemj00314-0269-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/d506e38c437f/biochemj00314-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e30/1144471/4230060ab88f/biochemj00314-0271-a.jpg

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本文引用的文献

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THE ELECTRON MICROSCOPY OF THE NORMAL HUMAN LENS.正常人晶状体的电子显微镜检查
Invest Ophthalmol. 1965 Aug;4:433-46.
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NEW CONCEPTS OF HUMAN LENTICULAR LIPIDS AND THEIR POSSIBLE ROLE IN CATARACTS.人类晶状体脂质的新概念及其在白内障形成中的可能作用
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The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes.人红细胞无血红蛋白空泡的制备及其化学特性
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Presence and localization of proteins immunologically related to erythrocyte protein 4.1 in human skin.与红细胞蛋白4.1免疫相关的蛋白质在人皮肤中的存在及定位
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Regional differences in the composition of the bovine lens urea-soluble protein.牛晶状体尿素可溶性蛋白组成的区域差异。
Exp Eye Res. 1980 Jan;30(1):109-13. doi: 10.1016/0014-4835(80)90129-3.
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Erythrocyte membrane skeletal protein bands 4.1 a and b are sequence-related phosphoproteins.红细胞膜骨架蛋白带4.1a和4.1b是序列相关的磷蛋白。
J Biol Chem. 1982 Apr 25;257(8):4564-9.
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Glycoproteins of lens membranes.晶状体膜糖蛋白
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Band 4.1 causes spectrin-actin gels to become thixiotropic.4.1带使血影蛋白-肌动蛋白凝胶变成触变的。
Biochem Biophys Res Commun. 1980 Dec 31;97(4):1429-35. doi: 10.1016/s0006-291x(80)80025-8.
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Spectrin-actin associations studied by electron microscopy of shadowed preparations.通过对投影标本进行电子显微镜观察研究血影蛋白与肌动蛋白的结合。
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