PEGylation Promotes Hemoglobin Tetramer Dissociation

2009 ◽  
Vol 20 (7) ◽  
pp. 1356-1366 ◽  
Author(s):  
Dario Caccia ◽  
Luca Ronda ◽  
Raffaella Frassi ◽  
Michele Perrella ◽  
Elena Del Favero ◽  
...  
Keyword(s):  
Hemoglobin Tetramer

scholarly journals A Twins Heritability Study on Alpha Hemoglobin Stabilizing Protein (AHSP) Expression Variability

2010 ◽  
Vol 13 (6) ◽  
pp. 567-572 ◽  
Author(s):  
Mei I. Lai ◽  
Chad Garner ◽  
Jie Jiang ◽  
Nicholas Silver ◽  
Steve Best ◽  
...  
Keyword(s):  
Protein Expression ◽  
Membrane Damage ◽  
Therapeutic Interventions ◽  
Ineffective Erythropoiesis ◽  
Red Cell Membrane ◽  
Cell Membrane Damage ◽  
Expression Variability ◽  
Hemoglobin Tetramer ◽  
Genetic Heritability

Cytotoxic precipitation of free α-globin monomers and its production of reactive oxygen species cause red cell membrane damage that leads to anemia and eventually ineffective erythropoiesis in β-thalassemia. Alpha hemoglobin stabilizing protein (AHSP) was found to bind only to free α-globin monomers creating a stable and inert complex which remains soluble in the cytoplasm thus preventing harmful precipitations. Alpha hemoglobin stabilizing protein was shown to bind nascent α-globin monomers with transient strength before transferring α-globin to β-globin to form hemoglobin tetramer. A classical twin study would be beneficial to investigate the role of genetics and environment in the variation of alpha hemoglobin stabilizing protein expression as this knowledge will enable us to determine further investigations with regards to therapeutic interventions if alpha hemoglobin stabilizing protein is to be a therapeutic agent for β-thalassemia. This study investigates the heritability influence of alpha hemoglobin stabilizing protein expression and factors that may contribute to this. Results indicated that a major proportion of alpha hemoglobin stabilizing protein expression was influenced by genetic heritability (46%) withcis-acting factors accounting for 19% andtrans-acting factors at 27%.

scholarly journals Hemoglobin Tetramer Measurement

2020 ◽  
Author(s):  
Keyword(s):  
Hemoglobin Tetramer

scholarly journals Enhanced survival of sickle erythrocytes upon treatment with glyceraldehyde

Blood ◽  
1986 ◽  
Vol 67 (2) ◽  
pp. 544-546 ◽  
Author(s):  
LJ Benjamin ◽  
JM Manning
Keyword(s):  
Life Span ◽  
Lysine Residue ◽  
Red Cell ◽  
Hemoglobin Tetramer ◽  
Sickle Erythrocytes ◽  
The Mean

Abstract Glyceraldehyde has been demonstrated to be an antisickling agent in vitro. In the present investigation, chromium-51 red cell studies were used to investigate the life span in vivo of sickle erythrocytes after treatment with glyceraldehyde in vitro. The mean survival (T1/2) of control cells was 5.8 +/- 1.6 days, whereas cells treated with 10 mmol/L or 20 mmol/L glyceraldehyde survived 9.0 +/- 1.4 (P less than .05) and 11.3 +/- 0.8 (P less than .002) days, respectively. The extent of modification by glyceraldehyde was 0.4 to 1.0 lysine residue per hemoglobin tetramer. These studies demonstrate not only a prolongation of the life span of sickle erythrocytes by treatment with glyceraldehyde but also the absence of any deleterious effects that would be revealed by this study.

scholarly journals LPS-Binding Sites On the Hemoglobin Tetramer - Prediction and Validation

2012 ◽  
Vol 102 (3) ◽  
pp. 65a
Author(s):  
Neha Bahl ◽  
Bruce Tidor ◽  
Jeak Ling Ding
Keyword(s):  
Binding Sites ◽  
Hemoglobin Tetramer ◽  
Lps Binding

A calorimetric study on the concentration dependent of hemoglobin tetramer assembly

2011 ◽  
Vol 44 (13) ◽  
pp. S94 ◽  
Author(s):  
Samaneh Zolghadri ◽  
Ali Akbar Saboury ◽  
Maliheh Sadat Atri
Keyword(s):  
Calorimetric Study ◽  
Hemoglobin Tetramer

Thermodynamic Stability of the Asymmetric Doubly-Ligated Hemoglobin Tetramer (α+CNβ+CN)(αβ):  Methodological and Mechanistic Issues†

Biochemistry ◽  
1997 ◽  
Vol 36 (36) ◽  
pp. 10822-10829 ◽  
Author(s):  
Gary K. Ackers ◽  
Michele Perrella ◽  
Jo M. Holt ◽  
Ilya Denisov ◽  
Yingwen Huang
Keyword(s):  
Thermodynamic Stability ◽  
Hemoglobin Tetramer

scholarly journals Symmetry distortion in the human hemoglobin tetramer induced by asymmetric ligation

FEBS Letters ◽  
2011 ◽  
Vol 586 (1) ◽  
pp. 74-78 ◽  
Author(s):  
Naoya Shibayama
Keyword(s):  
Human Hemoglobin ◽  
Hemoglobin Tetramer

Intersubunit circular permutation of human hemoglobin

Blood ◽  
2002 ◽  
Vol 100 (1) ◽  
pp. 299-305 ◽  
Author(s):  
Kevin E. Sanders ◽  
John Lo ◽  
Stephen G. Sligar
Keyword(s):  
Oxygen Affinity ◽  
Gene Synthesis ◽  
Human Hemoglobin ◽  
Central Cavity ◽  
Alpha Chain ◽  
Hemoglobin Tetramer ◽  
Novel Method ◽  
Expression Inescherichia Coli ◽  
Very High ◽  
Potential Oxygen

Abstract For many years, human hemoglobin (Hb) isolated from erythrocytes has been investigated as a potential oxygen delivery therapeutic. Advantages with respect to the need for blood typing were balanced with various undesirable properties of cell-free Hb, including cost, overall oxygen affinity, alterations in cooperativity, and ready dissociation into toxic dimeric species. The use of total gene synthesis has resulted in very high levels of functional human Hb expression inEscherichia coli, but there remains a desire for effecting the crosslinking of the hemoglobin tetramer and providing for ready means for increasing the globular molecular weight. In this communication, we report a novel method for linking alpha chains. By circularly permuting one alpha sequence, the second alpha chain in the Hb tetramer can be linked with glycine residues to form 2 bridges across the central cavity. The second alpha chain thus presents its amino and carboxyl termini on a solvent exposed surface, providing for additional polymerization of oxygen-carrying subunits or attachment of any other peptide-based therapeutic.

scholarly journals Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function

2002 ◽  
Vol 99 (15) ◽  
pp. 9777-9782 ◽  
Author(s):  
G. K. Ackers ◽  
P. M. Dalessio ◽  
G. H. Lew ◽  
M. A. Daugherty ◽  
J. M. Holt
Keyword(s):  
Hemoglobin Tetramer
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