Hemoglobin lufkin: Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue

Robert M. Schmidt; Katherine C. Bechtel; Mary H. Johnson; Bradford L. Therrell; Winston F. Moo-Penn

doi:10.3109/03630267709003908

Hemoglobin lufkin: Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue

Robert M. Schmidt, Katherine C. Bechtel, Mary H. Johnson, Bradford L. Therrell, Winston F. Moo-Penn

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

20 Scopus citations

Abstract

Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the β chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65°C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.

Original language	English (US)
Pages (from-to)	799-814
Number of pages	16
Journal	Hemoglobin
Volume	1
Issue number	8
DOIs	https://doi.org/10.3109/03630267709003908
State	Published - 1977
Externally published	Yes

ASJC Scopus subject areas

Hematology
Clinical Biochemistry
Genetics(clinical)
Biochemistry, medical

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title = "Hemoglobin lufkin: Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue",

abstract = "Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the β chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65°C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.",

author = "Schmidt, {Robert M.} and Bechtel, {Katherine C.} and Johnson, {Mary H.} and Therrell, {Bradford L.} and Moo-Penn, {Winston F.}",

year = "1977",

doi = "10.3109/03630267709003908",

language = "English (US)",

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TY - JOUR

T1 - Hemoglobin lufkin

T2 - Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue

AU - Schmidt, Robert M.

AU - Bechtel, Katherine C.

AU - Johnson, Mary H.

AU - Therrell, Bradford L.

AU - Moo-Penn, Winston F.

PY - 1977

Y1 - 1977

N2 - Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the β chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65°C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.

AB - Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the β chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65°C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.

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Hemoglobin lufkin: Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue

Abstract

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