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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. 1980
A Tsapis, and
N Hinard, and
U Testa, and
A Dubart, and
W Vainchenker, and
P Rouyer-Fessard, and
Y Beuzard, and
J Rosa
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.
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