Functional properties of hemoglobins in the teleostTilapia grahami

Autor:	Geoffrey M. O. Maloiy, Kjell Johansen, Gunnar Lykkeboe
Rok vydání:	1975
Předmět:	food.ingredient Chromatography GTP' Physiology Alkalinity Tilapia Biology Biochemistry Chloride Endocrinology food Ionic strength medicine Biophysics Animal Science and Zoology Hemoglobin Nucleoside Ecology Evolution Behavior and Systematics Oxygen binding medicine.drug
Zdroj:	Journal of Comparative Physiology B. 104:1-11
ISSN:	1432-136X 0340-7616
DOI:	10.1007/bf02482832
Popis:	The oxygen binding properties ofTilapia grahami hemoglobins have been investigated. The whole blood hemolysate possesses at 35°C a high oxygen affinity (P 50∼ 4.0 mmHg). The O2Hb equilibrium is moderately affected by the ionic strenght chloride concentration) of the hemoglobin solution, while in contrast the temperature sensitivity of the O2Hb equilibrium was very high (ΔH=−20.0 kcal.mole−1). Tilapia hemoglobin separated into 7 main fractions having nearly similar Bohr factors (−0.42
Databáze:	OpenAIRE
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