Hemoglobins from bats (Myotis myotis and Rousettus aegyptiacus): a possible example of molecular adaptation to different physiological requirements.
The functional properties of the hemoglobin systems from two different species of bat i.e. Rousettus aegyptiacus and Myotis myotis have been studied as a function of chloride, polyphosphates, pH and temperature. Apart from overall similarities shared with most mammalian hemoglobins, the two systems show significant differences with respect to the effect of chloride and temperature sensitivity. These findings have been related to the different physiological needs of the two species.
Condò
S G
SG
Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Italy.
el-Sherbini
S
S
Shehata
Y M
YM
Corda
M
M
Pellegrini
M G
MG
Brix
O
O
Giardina
B
B
D000818:Animals; D002685:Chiroptera / Q000097:blood*; D004734:Energy Metabolism; D006454:Hemoglobins / Q000032:analysis*; D006461:Hemolysis; D006863:Hydrogen-Ion Concentration; D010100:Oxygen / Q000097:blood; D013045:Species Specificity; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D010100:Oxygen