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人红细胞单糖转运系统中细胞松弛素B结合成分的纯化

Purification of the cytochalasin B binding component of the human erythrocyte monosaccharide transport system.

作者信息

Baldwin S A, Baldwin J M, Gorga F R, Lienhard G E

出版信息

Biochim Biophys Acta. 1979 Mar 23;552(1):183-8. doi: 10.1016/0005-2736(79)90257-8.

Abstract

The cytochalasin B binding component of the human erythrocyte monosaccharide transport system has been purified. The preparation appears to contain one major protein with an apparent polypeptide chain molecular weight of 55,000 and about 0.4 binding sites per chain. Cytochalasin B binds to the reconstituted preparation with a dissociation constant of 1.3.10(-7) M, a value which is similar to that reported for the transport system in the intact erythrocyte.

摘要

人红细胞单糖转运系统的细胞松弛素B结合成分已被纯化。该制剂似乎含有一种主要蛋白质,其表观多肽链分子量为55,000,每条链约有0.4个结合位点。细胞松弛素B以1.3×10⁻⁷ M的解离常数与重构制剂结合,该值与完整红细胞中转运系统的报道值相似。

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