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

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 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

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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",

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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.

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AN - SCOPUS:0014492797

SN - 0022-2143

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JO - The Journal of Laboratory and Clinical Medicine

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IS - 4

ER -

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

Abstract

ASJC Scopus subject areas

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