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A study was made of the Hb phenotype of the Sardinian dwarfhorse (Equus caballus jara), one of the last surviving wild horse species in Europe. Hb haplotypes and their frequencies were found to be similar to those described in the Arabian horse (BI = 0.551, BII = 0.389, A = 0.036, V = 0.015), which suggests possible introduction onto the island from North Africa. The oxygen binding properties of the whole hemolysates and of the four different horse Hbs, separated by ion-exchange chromatography, were considered with regard to the effect of chloride, 2,3-bisphosphoglycerate and lactate. Results indicate that no differences exist in the four components that characterize horse Hb. The molecular basis of the intrinsically low oxygen affinity and of the weak interaction of horse Hb with 2,3-bisphosphoglycerate is discussed in the light of the primary structure of the molecule.

It has been generally assumed that mammals have blood with a greater temperature sensitivity than ectothermic organisms. Recent results have shown that in some species of mammals, Hb displays a value of overall oxygenation enthalpy (delta H) much less exothermic than that observed for most mammalian hemoglobins, including human adult Hb. In this respect, a very interesting case is represented by porcine blood which shows a modest effect of temperature, the temperature coefficient of its oxygen-dissociation curve being significantly lower than that of human blood. Here we report a detailed functional characterization of pig Hb, which, interpreted on the basis of the amino acid sequence of the alpha and beta chains of the molecule, sheds some light on the molecular basis of the phenomenon.

Birds during normal sustained flight must be able to dissipate more than 8 times as much heat as during rest in order not to be overheated. The experiments reported in this note on the hemoglobin systems from two different birds indicate the existence of a molecular mechanism by which hemoglobin is used simultaneously for oxygen transport and heat dissipation.

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.