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EVOLUTION OF RUMINANT HEMOGLOBINS - THERMODYNAMIC DIVERGENCE OF OX AND BUFFALO HEMOGLOBINS

GIARDINA, B ; AREVALO, F ; CLEMENTI, ME ; FERRARA, L ; DILUCCIA, A ; LENDARO, E ; BELLELLI, A ; CONDO, SG

European journal of biochemistry, 1992-03, Vol.204 (2), p.509-513 [Periódico revisado por pares]

HOBOKEN: Wiley

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Título:
EVOLUTION OF RUMINANT HEMOGLOBINS - THERMODYNAMIC DIVERGENCE OF OX AND BUFFALO HEMOGLOBINS
Autor: GIARDINA, B ; AREVALO, F ; CLEMENTI, ME ; FERRARA, L ; DILUCCIA, A ; LENDARO, E ; BELLELLI, A ; CONDO, SG
Assuntos: Analytical, structural and metabolic biochemistry ; Animals ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Bubalus bubalis ; cattle ; evolution ; Fundamental and applied biological sciences. Psychology ; haemoglobin ; Hemoglobins - genetics ; Hemoglobins - metabolism ; Hemoproteins ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Life Sciences & Biomedicine ; Metalloproteins ; Oxygen - metabolism ; Phenotype ; Proteins ; Ruminants - genetics ; Science & Technology ; Thermodynamics
É parte de: European journal of biochemistry, 1992-03, Vol.204 (2), p.509-513
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The ligand-binding properties of hemoglobins from two homozygote phenotypes (AA and BB) of water buffalo (Bubalus bubalis) have been characterized by equilibrium and kinetic techniques. In the case of the BB phenotype, the two constituent hemoglobins have been purified and separately analysed. Buffalo hemoglobins display the reduced sensitivity to organic phosphates characteristic of ruminant hemoglobins, their physiological effector probably being the chloride ion. In contrast to the other known hemoglobins from ruminants, all the hemoglobins from the water buffalo display a significant temperature sensitivity, the DELTA-H for oxygen binding in the presence of physiological effectors approaching that of human hemoglobin (DELTA-H = -30.5 kJ/mol O2). This discrepancy with the other ruminant hemoglobins (e.g. ox, DELTA-H = -10.4 kJ/mol O2), whose primary structure is very similar to that of buffalo, hemoglobins might be correlated to the different habitat and phylogenetic history of the two subfamilies (Bos and Bubalus) of Bovidae.
Editor: HOBOKEN: Wiley
Idioma: Inglês

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EVOLUTION OF RUMINANT HEMOGLOBINS - THERMODYNAMIC DIVERGENCE OF OX AND BUFFALO HEMOGLOBINS

GIARDINA, B ; AREVALO, F ; CLEMENTI, ME ; FERRARA, L ; DILUCCIA, A ; LENDARO, E ; BELLELLI, A ; CONDO, SG

HOBOKEN: Wiley

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