On the oxygen-linked anion-binding sites in human hemoglobin. Functional properties of human hemoglobin reacted with 4-isothiocyanatobenzenesulphonic acid and its hybrids-Reference-Cited by-同舟云学术

On the oxygen-linked anion-binding sites in human hemoglobin. Functional properties of human hemoglobin reacted with 4-isothiocyanatobenzenesulphonic acid and its hybrids

Published:1986-12 Issue:2 Volume:161 Page:329-333
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

BELLELLE Andrea,IPPOLITI Rodolfo,CURRELL Douglas,CONDO Saverio G.,GIARDINA Bruno,BRUNORI Maurizio

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1986.tb10451.x/fullpdf

Reference25 articles.

1. X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1 alpha.

2. Identification of Chloride-Binding Sites in Hemoglobin by Nuclear-Magnetic-Resonance Quadrupole-Relaxation Studies of Hemoglobin Digests

3. 3. C. Bonaventura, and J. Bonaventura (1978 ) Biochemical and clinical aspects of hemoglobin , pp.647 -663 , Academic Press, New York.

4. Oxygen-linked binding sites for inorganic anions to hemoglobin.

5. The effect of 4-isothiocyanatobenzene sulfonic acid on the oxygen affinity of human hemoglobin

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