Allosteric Effect of 0-Iodobenzoate on Hemoglobin
作者:
TaketaF.,
ChenJ. Y.,
SkogenW. F.,
LitwinS. B.,
LaverM. B.,
期刊:
Hemoglobin
(Taylor Available online 1978)
卷期:
Volume 2,
issue 3
页码: 261-273
ISSN:0363-0269
年代: 1978
DOI:10.3109/03630267809007071
出版商: Taylor&Francis
数据来源: Taylor
摘要:
o-lodobenzoate interacts non-covalently with hemoglobin and lowers the oxygen affinity of the protein. In contrast to2,3diphosphoglycerate or inositol hexaphosphate, its interaction does not depend upon the presence of free amino groups at theβ-chain amino terminals. Lysineβ82 is one of its oxygenation linked binding sites. As with the organic phosphates, the halogenated benzoate reacts preferentially with deoxy-hemoglobin to shift the allosteric equilibrium from R to T.
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