Inhibition of Oxygen-Linked Anion Binding in Hb Camperdown [α2β2L04(G6)Arg→Ser]
作者:
KisterJ.,
BarbadjianJ.,
BlouquitY.,
BohnB.,
GalacterosF.,
PoyartC.,
期刊:
Hemoglobin
(Taylor Available online 1989)
卷期:
Volume 13,
issue 6
页码: 567-578
ISSN:0363-0269
年代: 1989
DOI:10.3109/03630268908993107
出版商: Taylor&Francis
数据来源: Taylor
摘要:
Oxygen equilibrium studies of purified Hb Camperdown [βl04(G6)Arg→Ser] have revealed an increased oxygen affinity at acid pH, while it is decreased for pH values above 7.4. This accounts for an almost 40% reduction in the alkaline Bohr effect. The effects of chloride and organophosphate effectors on the oxygen affinity of Hb Camperdown are inhibited by 40-50%. in chloridefree Hepes buffer, Hb Camperdown exhibits a lower oxygen affinity than normal Hb A. The present results confirm the important role of the positively charged residues lining theβ1β2interface in regulating the functional properties of hemoglobin.
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