Polymerization and Solubility of Recombinant Hemoglobinsα2β26VAL(HB S) andα2β26LEU(HB LEU)
作者:
AdachiK.,
RappaportE.,
EckH. S.,
KonitzerP.,
KimJ.,
SurreyS.,
期刊:
Hemoglobin
(Taylor Available online 1991)
卷期:
Volume 15,
issue 5
页码: 417-430
ISSN:0363-0269
年代: 1991
DOI:10.3109/03630269108998861
出版商: Taylor&Francis
数据来源: Taylor
摘要:
In an effort to clarify the role of amino acid hydrophobicity at theβ6 position in sickling we have made recombinant hemoglobin tetramers containingβ6 Val (Hb S) andβ6 Leu (Hb Leu). Recombinant Hb S and Hb Leu had the same electrophoretic mobility, chromatographic behavior, and absorption spectrum. The deoxy form of both tetramers polymerized in high phosphate buffer (1.8 M) and exhibited distinct delay times prior to polymerization. The kinetics of polymerization.for recombinant and native Hb S were similar, while recombinant Hb Leu polymerized more readily. The solubility of deoxy Hb Leu was less than deoxy Hb S, indicating that rapid polymerization and decreased solubility of deoxyhemoglobin is accelerated with increasing hydrophobicity at theβ6 position.
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