Hemoglobin P (α2β2117 Arg): Structure and properties

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

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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
Issue number4
StatePublished - Apr 1969

ASJC Scopus subject areas

  • Pathology and Forensic Medicine


Dive into the research topics of 'Hemoglobin P (α2β2117 Arg): Structure and properties'. Together they form a unique fingerprint.

Cite this