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用曲拉通X-100溶解人红细胞膜糖蛋白

Solubilization of human erythrocyte membrane glycoproteins by triton X-100.

作者信息

Pratt R S, Cook G M

出版信息

Biochem J. 1979 May 1;179(2):299-303. doi: 10.1042/bj1790299.

Abstract
  1. The enzymic removal of sialic acid residues from the glycoproteins of the human erythrocyte decreases the solubilization of membrane glycoprotein by Triton X-100. 2. The solubilization of asialoglycoprotein by Triton X-100 may be restored by the addition of borate. 3. Use of this non-ionic detergent in the presence of borate, as a general procedure for the mild solubilization of membrane glycoproteins deficient in sialic acid residues, is discussed.
摘要
  1. 从人红细胞糖蛋白上酶促去除唾液酸残基会降低Triton X-100对膜糖蛋白的增溶作用。2. 添加硼酸盐可恢复Triton X-100对去唾液酸糖蛋白的增溶作用。3. 讨论了在硼酸盐存在下使用这种非离子型去污剂作为温和增溶缺乏唾液酸残基的膜糖蛋白的通用方法。

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Integral membrane protein interaction with Triton cytoskeletons of erythrocytes.
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[Extraction and purification of the chief glycoprotein of the erythrocyte membrane].
Rev Fr Transfus Immunohematol. 1979 Sep;22(4):329-41. doi: 10.1016/s0338-4535(79)80029-x.

本文引用的文献

10
Human erythrocyte membrane sialoglycoproteins: a study of interconversion.人红细胞膜唾液酸糖蛋白:相互转化的研究
Biochem Biophys Res Commun. 1974 Jul 10;59(1):352-60. doi: 10.1016/s0006-291x(74)80214-7.

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