PURIFICATION OF STROMA-FREE HAEMOGLOBIN BY ATP-AGAROSE AFFINITY CHROMATOGRAPHY

Authors
  1. Hsia, J.C.
  2. Er, S.S.
Corporate Authors
Defence and Civil Inst of Environmental Medicine, Downsview ONT (CAN)
Abstract
Affinity chromatography has been shown to be one of the most powerful purification techniques available for the purification of biomacromolecules. Mammalian haemoglobin is known to have a diphosphoglycerate (DPG) binding site and avian haemoglobin is known to have an inositol pentaphosphate binding site. The binding of the polyphosphate allosterically affects the conformation of haemoglobin, leading to a lowered oxygen affinity. Conversely, binding of oxygen or carbon monoxide to the haeme moiety results in an allosteric conformation change which in turn lowers the affinity of the haemoglobin for the polyanions. Oxyhaemoglobin is known to bind DPG and ATP weakly. This communication explores the utility of this binding specificity for polyanionic ligands in the isolation and purification of haemoglobin.
Report Number
DCIEM-85-P-35 — Research Paper, Enviromedicine Publication; Chrombio.-2825
Date of publication
15 Aug 1985
Number of Pages
7
Reprinted from
J of Chromatography, no 374, 1986, p 143-148
DSTKIM No
86-01430
CANDIS No
96174
Format(s):
Hardcopy;Originator's fiche received by DSIS

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