Hemoglobin P (α2β2 117 Arg)

Structure and properties

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

Research output: Contribution to journalArticle

31 Citations (Scopus)

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 1969

Fingerprint

Histidine
Structural analysis
Arginine
Hydrogen
Hydrogen bonds
Substitution reactions
Erythrocytes
Molecules
hemoglobin P

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Medicine(all)

Cite this

Schneider, R. G., Alperin, J. B., Brimhall, B., & Jones, R. T. (1969). Hemoglobin P (α2β2 117 Arg): Structure and properties. The Journal of Laboratory and Clinical Medicine, 73(4), 616-622.

Hemoglobin P (α2β2 117 Arg) : Structure and properties. / Schneider, Rose G.; Alperin, Jack B.; Brimhall, Bernadine; Jones, Richard T.

In: The Journal of Laboratory and Clinical Medicine, Vol. 73, No. 4, 04.1969, p. 616-622.

Research output: Contribution to journalArticle

Schneider, RG, Alperin, JB, Brimhall, B & Jones, RT 1969, 'Hemoglobin P (α2β2 117 Arg): Structure and properties', The Journal of Laboratory and Clinical Medicine, vol. 73, no. 4, pp. 616-622.
Schneider RG, Alperin JB, Brimhall B, Jones RT. Hemoglobin P (α2β2 117 Arg): Structure and properties. The Journal of Laboratory and Clinical Medicine. 1969 Apr;73(4):616-622.
Schneider, Rose G. ; Alperin, Jack B. ; Brimhall, Bernadine ; Jones, Richard T. / Hemoglobin P (α2β2 117 Arg) : Structure and properties. In: The Journal of Laboratory and Clinical Medicine. 1969 ; Vol. 73, No. 4. pp. 616-622.
@article{6a4f4870c4904d29bd48aa186926560d,
title = "Hemoglobin P (α2β2 117 Arg): Structure and properties",
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.",
author = "Schneider, {Rose G.} and Alperin, {Jack B.} and Bernadine Brimhall and Jones, {Richard T.}",
year = "1969",
month = "4",
language = "English (US)",
volume = "73",
pages = "616--622",
journal = "Translational Research",
issn = "1931-5244",
publisher = "Mosby Inc.",
number = "4",

}

TY - JOUR

T1 - Hemoglobin P (α2β2 117 Arg)

T2 - Structure and properties

AU - Schneider, Rose G.

AU - Alperin, Jack B.

AU - Brimhall, Bernadine

AU - Jones, Richard T.

PY - 1969/4

Y1 - 1969/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0014492797&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014492797&partnerID=8YFLogxK

M3 - Article

VL - 73

SP - 616

EP - 622

JO - Translational Research

JF - Translational Research

SN - 1931-5244

IS - 4

ER -