|
|
 Previous Article | Table of Contents | Next Article 
Hemoglobin M equon beta 41 (C7) phenylalanine leads to tyrosine
LB Burkert, VS Sharma, AV Pisciotta, HM Ranney and S Bruckheimer
A severe hemolytic crisis was observed in a 34-yr-old female of English-
Irish extraction following a viral illness treated with acetaminophen.
Heinz bodies and heat instability were present only during a transient
hemolytic event. A challenge dose of acetaminophen caused no detectable
hematologic abnormality. Structural studies of the hemoglobin during
hemolysis and again after complete recovery localized the abnormality to
tryptic peptide beta Tp-5, and automated sequencing of I 125-labeled beta
chains indicated a replacement of phenylalanine (C7) beta 41 by tyrosine.
Substitution of the next residue, phenylalanine (CD1) beta 42 by serine (Hb
Hammersmith), has resulted in chronic severe Heinz body hemolytic anemia.
The lack of chronic anemia in the present disorder may reflect the
different relationships of beta41 and beta 42 and/or the similarities in
volume and hydrophobicity of tyrosine and phenylalanine. It is suggested
that substitution of tyrosine for phenylalanine in Hb Mequon may disturb
the critical environment around the heme group and render it susceptible to
oxidative denaturation in the presence of infections and/or drugs.
Volume 48,
Issue 5,
pp. 645-651,
11/01/1976
Copyright © 1976 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
B. J. Reeder, M. Grey, R.-L. Silaghi-Dumitrescu, D. A. Svistunenko, L. Bulow, C. E. Cooper, and M. T. Wilson
Tyrosine Residues as Redox Cofactors in Human Hemoglobin: IMPLICATIONS FOR ENGINEERING NONTOXIC BLOOD SUBSTITUTES
J. Biol. Chem.,
November 7, 2008;
283(45):
30780 - 30787.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
V. Baudin-Creuza, C. Vasseur-Godbillon, N. Griffon, J. Kister, L. Kiger, C. Poyart, M. C. Marden, and J. Pagnier
Additive Effects of beta Chain Mutations in Low Oxygen Affinity Hemoglobin beta F41Y,K66T
J. Biol. Chem.,
September 3, 1999;
274(36):
25550 - 25554.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. Griffon, C. Badens, D. Lena-Russo, J. Kister, J. Bardakdjian, H. Wajcman, M. C. Marden, and C. Poyart
Hb Bruxelles, Deletion of Phebeta 42, Shows a Low Oxygen Affinity and Low Cooperativity of Ligand Binding
J. Biol. Chem.,
October 18, 1996;
271(42):
25916 - 25920.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
