Acylation of Hemoglobin by Glutarylsalicylamide and Its Effect on Oxygen Transport Properties
作者:
TamJoseph W.O.,
期刊:
Hemoglobin
(Taylor Available online 1978)
卷期:
Volume 2,
issue 2
页码: 101-116
ISSN:0363-0269
年代: 1978
DOI:10.3109/03630267809074778
出版商: Taylor&Francis
数据来源: Taylor
摘要:
Hemoglobin A was modified in vitro with 0.02—0.03 M glutarylsalicylamide for two hours at pH 7.2 and 37°C. The extent of modification was about 30—50%, as estimated by visual comparison after electrophoretic separation. A substantial decrease in oxygen affinity of modified hemoglobin solutions was observed. Similar results were also obtained for dilute cell suspensions of washed red blood cells and whole blood after GSM modification. Other properties such as cooperativity, Bohr effect and 2,3-DPG dependence remained essentially unchanged. Although the site(s) of modification have not been determined, it is unlikely that they would involve any amino acid residue contributing to the above allosteric properties.
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