Red cell organic phosphates and Bohr effects in house sparrow blood

1985 ◽  
Vol 59 (1) ◽  
pp. 93-103 ◽  
Author(s):  
Leigh A. Maginniss
Keyword(s):  
House Sparrow ◽  
Red Cell ◽  
Organic Phosphates ◽  
Red Cell Organic Phosphates

THE SHIFT TO THE LEFT

PEDIATRICS ◽  
1971 ◽  
Vol 48 (6) ◽  
pp. 853-856 ◽  
Author(s):  
Frank A. Oski ◽  
Maria Delivoria-Papadopoulos
Keyword(s):  
Oxygen Transport ◽  
Normal Adult ◽  
Red Cell ◽  
Equilibrium Curve ◽  
Organic Phosphates ◽  
Clinical Interest ◽  
Red Cell Organic Phosphates

For many years it appeared that physiologists, and physiologists alone, puzzled over the causes and significance of alterations in the position of the oxygen-hemoglobin equilibrium curve. The reports by Benesch and Benesch1 and Chanutin and Curnish2 in 1967, concerning the role of red cell organic phosphates in determining the affinity of hemoglobin for oxygen, have served to rekindle curiosity in this problem of oxygen transport and produced a common focus of clinical interest for neonatologists, hematologists, biochemists, and the now nearly forgotten physiologists. The oxygen-hemoglobin equilibrium curve of normal adult blood is depicted as the center curve in Figure 1.

The Effect of Anti A Antibody on Red Cell Organic Phosphates and Adenosine Triphosphatase Activity in vitro

2009 ◽  
Vol 5 (3) ◽  
pp. 191-210 ◽  
Author(s):  
Jiří Palek ◽  
Libuše Mirčevová ◽  
Václav Brabec ◽  
Brfzřich Friedmann ◽  
Alexej Májský
Keyword(s):  
Adenosine Triphosphatase ◽  
Red Cell ◽  
Adenosine Triphosphatase Activity ◽  
Organic Phosphates ◽  
Red Cell Organic Phosphates

scholarly journals Organic phosphates increase the solubility of avian haemoglobin D and embryonic chicken haemoglobin

1984 ◽  
Vol 217 (3) ◽  
pp. 767-771 ◽  
Author(s):  
R Baumann ◽  
E Goldbach ◽  
E A Haller ◽  
P G Wright
Keyword(s):  
Ionic Strength ◽  
Stoichiometric Ratio ◽  
Red Cell ◽  
Physiological Temperature ◽  
Organic Phosphates ◽  
Functional Homology ◽  
Embryonic Chicken ◽  
Crystalline Aggregates

The isolated minor haemoglobin fractions (haemoglobin D) of ostrich, chicken and duck haemoglobin, which constitute about 30% of total intracellular haemoglobin, form crystalline aggregates upon deoxygenation at physiological temperature, ionic strength and pH and at haemoglobin concentrations even well below those present in the red cell. The aggregation is reversed by oxygenation, and can be inhibited by addition of organic phosphates or the corresponding major haemoglobin fraction in a stoichiometric ratio of 1:1. Embryonic haemoglobin from chicken has similar characteristics with respect to its solubility. The results indicate close functional homology of alpha D and embryonic pi-chains as well as a novel role for organic phosphates in the regulation of haemoglobin function.

The orientation of sickle hemoglobin fibers within fascicles

1988 ◽  
Vol 46 ◽  
pp. 400-401
Author(s):  
Christopher A. Miller ◽  
Bridget Carragher ◽  
William A. McDade ◽  
Robert Josephs
Keyword(s):  
Sickle Cell ◽  
Sickle Cell Anemia ◽  
Relative Orientation ◽  
Unit Cell ◽  
Red Cell ◽  
High Ph ◽  
Sickle Hemoglobin ◽  
Polar Crystal ◽  
Helical Configuration

Highly ordered bundles of deoxyhemoglobin S (HbS) fibers, termed fascicles, are intermediates in the high pH crystallization pathway of HbS. These fibers consist of 7 Wishner-Love double strands in a helical configuration. Since each double strand has a polarity, the odd number of double strands in the fiber imparts a net polarity to the structure. HbS crystals have a unit cell containing two double strands, one of each polarity, resulting in a net polarity of zero. Therefore a rearrangement of the double strands must occur to form a non-polar crystal from the polar fibers. To determine the role of fascicles as an intermediate in the crystallization pathway it is important to understand the relative orientation of fibers within fascicles. Furthermore, an understanding of fascicle structure may have implications for the design of potential sickling inhibitors, since it is bundles of fibers which cause the red cell distortion responsible for the vaso-occlusive complications characteristic of sickle cell anemia.

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