Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin

Measurements of oxygen binding to bovine hemoglobin have been carried out over the temperature range 15-37 degrees C at pH 7.33. The standard enthalpy of oxygenation after correction for the heat of oxygen solution and of the Bohr protons is found to be -7.1 or -7.2 kcal/mol in the presence of 0.1 M chloride or bromide, respectively. This value is well below the -14.4 kcal/mol determined for human hemoglobin under identical experimental conditions. As reported by Fronticelli et al. (C. Fronticelli, E. Bucci and A. Razynska, J. Mol. Biol. 202 (1988) 343), the preferential binding of anions by bovine hemoglobin recognizes the various halides. Measurements at various temperatures reveal that this is true only above 25 degrees C. The halide recognition and the less exothermic enthalpy of oxygenation of bovine hemoglobin are probable due to oxygen-linked hydrophobic effects that are larger in bovine than in human hemoglobin.     

Hemoglobins, XXI: sequence analysis of porcine hemoglobin (author's transl)

The hemoglobin of a bavarian domestic pig (Suidae) was isolated. The chains were separated by countercurrent distribution, then cleaved with trypsin. The isolated peptides were sequenced with hydrophilic phenylisothiocyanate I and IV, or with a dimethylaminopropyne program in the sequenator. The sequences of the chains are given. Some methodical aspects of automatic sequencing are discussed and the sequences of human porcine hemoglobin are compared. The role of adult pig haemoglobin as foetal hemoglobin is discussed.     

Hemoglobin XXIII: note on the sequence of the delta-chains of human hemoglobin (author's transl)

The minor component of the human adult hemoglobin Hb A2 (alpha2/delta2) was isolated. The peptide chains were separated by counter current distribution, the delta-chains digested with trypsin and all hydrolysis splitting products separated and quantitatively characterized. With the film technique the different peptides were sequenced with hydrophilic phenylisothiocyanates I and IV or by the propyne programme. The complete sequence of the delta-chains is given and compared with the sequence reported in former investigations, in which the delta-chain sequence was only partly elucidated. Having completely sequenced the delta-chains of the human hemoglobin, we found the 10 previously reported exchanges and no additional exchanges with respect to the beta-chains.