Equilibrium and kinetic studies of hemoglobin I: A functionally silent amino acid substitution at an invariant residue

M. J. McDonald; Robert W. Noble; V. S. Sharma; Helen M. Ranney

doi:10.1016/0022-2836(74)90175-2

Equilibrium and kinetic studies of hemoglobin I: A functionally silent amino acid substitution at an invariant residue

M. J. McDonald
, Robert W. Noble
, V. S. Sharma
, Helen M. Ranney

Medicine

SUNY Buffalo
University of California at San Diego

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

1 Scopus citations

Abstract

Hemoglobin I is an uncommon hemoglobin variant in which the lysine residue at position 16 of the a chain has been replaced by glutamic acid. Lysine is the invariant residue in all myoglobin and hemoglobin subunits that have been sequenced, with the exception of the hemoglobin of the lamprey. Replacement of invariant residues is generally reflected in altered functional properties of the hemoglobin molecule and such invariance may be indicative of a unique functional role. However, a study of the oxygen equilibrium and kinetic properties of hemoglobin I showed the functional properties of this hemoglobin to be indistinguishable from those of normal adult hemoglobin.

Original language	English
Pages (from-to)	245-248
Number of pages	4
Journal	Journal of Molecular Biology
Volume	89
Issue number	1
DOIs	https://doi.org/10.1016/0022-2836(74)90175-2
State	Published - Oct 15 1974

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abstract = "Hemoglobin I is an uncommon hemoglobin variant in which the lysine residue at position 16 of the a chain has been replaced by glutamic acid. Lysine is the invariant residue in all myoglobin and hemoglobin subunits that have been sequenced, with the exception of the hemoglobin of the lamprey. Replacement of invariant residues is generally reflected in altered functional properties of the hemoglobin molecule and such invariance may be indicative of a unique functional role. However, a study of the oxygen equilibrium and kinetic properties of hemoglobin I showed the functional properties of this hemoglobin to be indistinguishable from those of normal adult hemoglobin.",

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T1 - Equilibrium and kinetic studies of hemoglobin I

T2 - A functionally silent amino acid substitution at an invariant residue

AU - McDonald, M. J.

AU - Noble, Robert W.

AU - Sharma, V. S.

AU - Ranney, Helen M.

PY - 1974/10/15

Y1 - 1974/10/15

N2 - Hemoglobin I is an uncommon hemoglobin variant in which the lysine residue at position 16 of the a chain has been replaced by glutamic acid. Lysine is the invariant residue in all myoglobin and hemoglobin subunits that have been sequenced, with the exception of the hemoglobin of the lamprey. Replacement of invariant residues is generally reflected in altered functional properties of the hemoglobin molecule and such invariance may be indicative of a unique functional role. However, a study of the oxygen equilibrium and kinetic properties of hemoglobin I showed the functional properties of this hemoglobin to be indistinguishable from those of normal adult hemoglobin.

AB - Hemoglobin I is an uncommon hemoglobin variant in which the lysine residue at position 16 of the a chain has been replaced by glutamic acid. Lysine is the invariant residue in all myoglobin and hemoglobin subunits that have been sequenced, with the exception of the hemoglobin of the lamprey. Replacement of invariant residues is generally reflected in altered functional properties of the hemoglobin molecule and such invariance may be indicative of a unique functional role. However, a study of the oxygen equilibrium and kinetic properties of hemoglobin I showed the functional properties of this hemoglobin to be indistinguishable from those of normal adult hemoglobin.

UR - https://www.scopus.com/pages/publications/0016140573

U2 - 10.1016/0022-2836(74)90175-2

DO - 10.1016/0022-2836(74)90175-2

M3 - Article

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AN - SCOPUS:0016140573

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SP - 245

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -

Equilibrium and kinetic studies of hemoglobin I: A functionally silent amino acid substitution at an invariant residue

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