Temperature modulation of bovine hemoglobins.
The functional properties of hemoglobin from Egyptian water buffalo have been characterized as a function of pH, temperature and chloride concentration. Alongside overall similarities shared with ox and Arctic ruminant hemoglobins, hemoglobin from buffalo shows significant differences with respect to the effect of temperature. The results obtained may suggest that the limited effect of temperature on oxygen binding recently reported for ox hemoglobin could be regarded as an interesting case of a reminiscence of a past glacial age.
Condò
S G
SG
Department of Experimental Medicine and Biochemical Sciences, University of Rome "Tor Vergata," Italy.
el-Sherbini
S
S
Giardina
B
B
D000818:Animals; D002020:Buffaloes / Q000097:blood; D002417:Cattle / Q000097:blood*; D003670:Deer / Q000097:blood; D006454:Hemoglobins / Q000378:metabolism*; D006736:Horses / Q000097:blood; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010108:Oxyhemoglobins / Q000378:metabolism*; D013045:Species Specificity; D013696:Temperature; D013816:Thermodynamics
D006454:Hemoglobins; D010108:Oxyhemoglobins