Hemoglobin heterogeneity and the oxygen affinity of the hemolysate of some Victoria cichlids.
The hemoglobin patterns of ten cichlid species from Lake Victoria were characterized by polyacrylamide gel electrophoresis. In all tested species the hemoglobin bands display the same electrophoretic mobility. Oxygen equilibria of the purified hemoglobin solution of five species were determined under standardized conditions (pH 7.4 at 20 degrees C). The analysed hemolysates have a relatively high oxygen affinity and for all the tested species the Hill coefficient approached unity. The effect of temperature on the oxygen affinity of Haplochormis "velvet black" hemolysate was determined at 20, 25, 30 and 35 degrees C. The obtained results (delta H value-68 kJ/mol) at pH 8.2 is comparable with earlier published results for other African and South American Cichlidae. The Bohr effect (phi = delta log P50/delta pH = -0.18 between pH 6.6-7.4 at 25 degrees C) proved to be lower than so far reported in other Cichlidae.
Verheyen
E
E
Blust
R
R
Decleir
W
W
D000818:Animals; D005399:Fishes / Q000097:blood*; D006454:Hemoglobins / Q000302:isolation & purification* / Q000378:metabolism; D006461:Hemolysis; D006863:Hydrogen-Ion Concentration; D010100:Oxygen / Q000097:blood; D010108:Oxyhemoglobins / Q000378:metabolism; D013045:Species Specificity
D006454:Hemoglobins; D010108:Oxyhemoglobins; D010100:Oxygen