Hemoglobin P (α2β2117 Arg): Structure and properties

Rose G. Schneider, Jack B. Alperin, Bernadine Brimhall, Richard T. Jones

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Structural analysis of hemoglobin P reveals a substitution of the histidine by an arginine residue at β 117, in the helical position G 19. In both subjects with Hgb. P trait there are slight morphologic abnormalities of the erythrocytes-hypochromia, anisopoikilocytosis, and targeting. These may reflect molecular instability due to a disturbance of the pattern of hydrogen bonds in the α1β1 region of the molecule.

Original languageEnglish (US)
Pages (from-to)616-622
Number of pages7
JournalThe Journal of Laboratory and Clinical Medicine
Volume73
Issue number4
StatePublished - Apr 1 1969

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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    Schneider, R. G., Alperin, J. B., Brimhall, B., & Jones, R. T. (1969). Hemoglobin P (α2β2117 Arg): Structure and properties. The Journal of Laboratory and Clinical Medicine, 73(4), 616-622.