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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Adachi, K. Articles by Schwartz, E. Search for Related Content PubMed PubMed Citation Articles by Adachi, K. Articles by Schwartz, E. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Characterization of two types of fetal hemoglobin: alpha 2G gamma 2 and alpha 2A gamma 2 K Adachi, J Kim, T Asakura and E Schwartz Division of Hematology, Children's Hospital of Philadelphia, University of Pennsylvania School of Medicine 19104. The effect of differences in G gamma and A gamma fractions of fetal hemoglobin (HbF) on the kinetics of polymerization of HbS-HbF mixtures was studied. We also examined their effect on oxygen affinity, surface hydrophobicity, mechanical stability, and solubility of HbF. Differences in G gamma:A gamma ratio did not affect the polymerization of mixtures of HbF and HbS, suggesting that the inhibitory effect of HbF on the polymerization of HbS is independent of the G gamma:A gamma ratio of HbF and is totally dependent on the fraction of HbF in the mixture. The oxygen equilibrium curve of HbF was not affected by differences in the ratios of G gamma and A gamma in HbF. In contrast, surface hydrophobicity, mechanical stability, and solubility of HbF were affected by differences in the G gamma:A gamma ratio. The higher the G gamma:A gamma ratio, the smaller the elution volume on a TSK Gel SW hydrophobic column in high phosphate buffer. The mechanical stability of HbF was also dependent on the ratio of G gamma:A gamma; stability was greater at higher fractions of A gamma. Differences in the G gamma:A gamma ratio also affected solubility of HbF: HbF containing the higher fraction of G gamma was the more soluble. These data indicate that although alanine at the 136th position of the gamma chains has a stronger surface hydrophobicity than does glycine, this difference does not affect either the polymerization of HbS or the oxygen affinity of HbF. Volume 75, Issue 10, pp. 2070-2075, 05/15/1990 Copyright © 1990 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: K. Adachi, J. Pang, L. R. Reddy, L. E. Bradley, Q. Chen, P. Trifillis, E. Schwartz, and S. Surrey Polymerization of Three Hemoglobin A2 Variants Containing Valdelta 6 and Inhibition of Hemoglobin S Polymerization by Hemoglobin A2 J. Biol. Chem., October 4, 1996; 271(40): 24557 - 24563. [Abstract] [Full Text] [PDF]

	Copyright © 1990 by American Society of Hematology         Online ISSN: 1528-0020