Hemoglobin P (α2β2117 Arg): Structure and properties

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

Hemoglobin P (α₂β₂^{117 Arg}): Structure and properties

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

Internal Medicine

Research output: Contribution to journal › Article › peer-review

33 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 language	English (US)
Pages (from-to)	616-622
Number of pages	7
Journal	The Journal of Laboratory and Clinical Medicine
Volume	73
Issue number	4
State	Published - Apr 1969

ASJC Scopus subject areas

Pathology and Forensic Medicine

Cite this

@article{6a4f4870c4904d29bd48aa186926560d,

title = "Hemoglobin P (α2β2117 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 = apr,

language = "English (US)",

volume = "73",

pages = "616--622",

journal = "The Journal of Laboratory and Clinical Medicine",

issn = "0022-2143",

publisher = "Elsevier Inc.",

number = "4",

}

TY - JOUR

T1 - Hemoglobin P (α2β2117 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 - https://www.scopus.com/pages/publications/0014492797

UR - https://www.scopus.com/pages/publications/0014492797#tab=citedBy

M3 - Article

C2 - 5775133

AN - SCOPUS:0014492797

SN - 0022-2143

VL - 73

SP - 616

EP - 622

JO - The Journal of Laboratory and Clinical Medicine

JF - The Journal of Laboratory and Clinical Medicine

IS - 4

ER -

Hemoglobin P (α₂β₂^{117 Arg}): Structure and properties

Abstract

ASJC Scopus subject areas

Other files and links

Fingerprint

Cite this