ISSN:
1439-0426
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
,
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Notes:
The oxygen binding properties of Acipenser naccarii hemoglobins have been investigated, and were found not to differ significantly from those shown by blood, intact erythrocytes and hemolysate in the presence of the physiological cofactors GTP and chloride ions. In particular, the oxygen equilibrium reveal a very low sensitivity of the hemolysate to the chloride ions and temperature while in the presence of organic phosphates their oxygen affinity decreased strongly. The electrophoretic analysis of the hemolysate of the sturgeon showed the presence of two hemoglobin components, each with a considerable globin multiplicity. The partial amino acid sequence of the a and P chain of the single hemoglobins was also established.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1439-0426.1999.tb00211.x
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