期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：5
页码：1506-1508
DOI：10.1073/pnas.70.5.1506
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Apparent weight-average molecular weights of hemoglobin A and hemoglobin S were measured at high concentrations by equilibrium ultracentrifugation. Carbonmonoxy-hemoglobin S appears to exist as a solution of unassociated molecules, as do carbonmonoxy-and deoxy-hemoglobin A. Deoxy-hemoglobin S, however, exists in a gel-like state at concentrations above 14 g/dl, but no aggregates smaller than the gel were observed in solutions that were in equilibrium with the gel. Carbamoylation of hemoglobin S produced a solution of unaggregated molecules, as did cooling of uncarbamoylated hemoglobin S to 5{degrees}. It is concluded that the gel of hemoglobin S is formed in a stoichiometrically concerted manner, and that the size of the smallest stable aggregate is greater than 20 hemoglobin molecules.
关键词：hemoglobin A ; sickle-cell anemia ; ultracentrifugation ; protein association
