基于琼脂糖结合珠蛋白的珠蛋白链亲和层析法：一种研究网织红细胞、骨髓及红系前体细胞集落中血红蛋白合成的新方法。

Globin-chain affinity chromatography on Sepharose-haptoglobin: a new method of study of hemoglobin synthesis in reticulocytes, in bone marrow and in colonies of erythroid precursors.

作者信息

Tsapis A, Hinard N, Testa U, Dubart A, Vainchenker W, Rouyer-Fessard P, Beuzard Y, Rosa J

出版信息

Eur J Biochem. 1980 Dec;112(3):513-9. doi: 10.1111/j.1432-1033.1980.tb06114.x.

DOI:10.1111/j.1432-1033.1980.tb06114.x

Abstract

In the present work we have developed an affinity chromatography system, using haptoglobin bound covalently to Sepharose 4B, to purify hemoglobin from soluble non-heme proteins. Sepharose-haptoglobin specifically binds hemoglobin. It exhibits the same characteristics in its interactions with hemoglobin and alpha or beta hemoglobin chains as does haptoglobin in solution. Globin chains can be eluted from the Sepharose-haptoglobin after removal of the heme. This method has allowed accurate measurements of globin-chain synthesis in blood and bone marrow samples and in culture of early erythroid precursors.

摘要

在本研究中，我们开发了一种亲和层析系统，该系统使用与琼脂糖4B共价结合的触珠蛋白，从可溶性非血红素蛋白中纯化血红蛋白。琼脂糖-触珠蛋白能特异性结合血红蛋白。它在与血红蛋白及α或β血红蛋白链的相互作用中表现出与溶液中的触珠蛋白相同的特性。去除血红素后，珠蛋白链可从琼脂糖-触珠蛋白上洗脱下来。该方法能够准确测量血液和骨髓样本以及早期红系前体细胞培养物中的珠蛋白链合成。