Open AccessLow‐temperature sensitivity and enhanced Bohr effect in red deer ( Cervus elaphus ) haemoglobin: a molecular adaptive strategy to life at high altitude and low temperature
Author(s) -
Pellegrini Mariagiuseppina,
Giardina Bruno,
Castagnola Massimo,
Olianas Alessandra,
Sanna Maria Teresa,
Fais Antonella,
Messana Irene,
Corda Marcella
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00210.x
Subject(s) - cervus elaphus , bohr effect , biology , oxygen , biochemistry , chemistry , biophysics , zoology , ecology , hemoglobin , organic chemistry , oxygen–haemoglobin dissociation curve
A study of the functional properties of haemoglobin from red deer ( Cervus elaphus ) whose habitat varies over a wide range of latitude, was performed. The oxygen‐binding properties of the most common haemoglobin phenotype from the species living in Sardinia were examined with particular attention to the effect of pH, chloride, 2,3‐bisphosphoglycerate and temperature. Results indicate that red deer haemoglobin, like all haemoglobins from ruminants so far examined, is characterized by a low intrinsic oxygen affinity, with chloride being its main physiological modulator in vivo . The functional results and the low temperature sensitivity of the oxygen affinity are discussed in the light of the amino acid sequence of closely related ruminant haemoglobins.