Possible adaptive significance of low red cell organic phosphates in crocodiles

1979 ◽  
Vol 209 (1) ◽  
pp. 161-167 ◽  
Author(s):  
Gordon C. Grigg ◽  
Margie Gruca
PEDIATRICS ◽  
1971 ◽  
Vol 48 (6) ◽  
pp. 853-856 ◽  
Author(s):  
Frank A. Oski ◽  
Maria Delivoria-Papadopoulos

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.


2009 ◽  
Vol 5 (3) ◽  
pp. 191-210 ◽  
Author(s):  
Jiří Palek ◽  
Libuše Mirčevová ◽  
Václav Brabec ◽  
Brfzřich Friedmann ◽  
Alexej Májský

1974 ◽  
Vol 82 (3) ◽  
pp. 563-566 ◽  
Author(s):  
B. P. Sengupta

SUMMARYThe possible adaptive significance of the occurrence of HK and LK red-cell types in Murrah buffaloes was investigated. Judged by haematological indices and thermorespiratory responses under conditions of moderate thermal stress, LK animals appeared to have a greater adaptive potential than HK animals in a hot arid environment. Dry matter percentage, packed cell volume (pcv), haemoglobin concentration (Hb), red blood corpuscles (RBC) and plasma protein values were significantly higher in LK-type animals. In addition, under identical conditions of thermal stress the LK animals exhibited significantly less rise in rectal temperature and respiratory rate than the HK animals.


1984 ◽  
Vol 217 (3) ◽  
pp. 767-771 ◽  
Author(s):  
R Baumann ◽  
E Goldbach ◽  
E A Haller ◽  
P G Wright

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.


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