Oxygen Binding Characteristics Of Daphnia Hemoglobin
January 1, 1990 - KOBAYASHI, M; FUJIKI, M; SUZUKI, T
Print
EmailJournal or Book Title: JOURNAL OF THERMAL BIOLOGY
Volume/Issue: 15
Year Published: 1990
The effects of temperature on the oxygen binding properties of Daphnia magna haemoglobin (Hb) solutions from Hb-rich and Hb-poor animals were examined at 10-20.degree. C. The apparent heats of oxygenation (.DELTA.H) of Daphnia magna Hb obtained from Hb-rich animals was -14.5 Kcal/mol, while that of Hb-poor animals was -7.0 Kcal/mol. Cooperativeity (Hill coefficient) ranged from 1.2 to 1.7, and was not effected by temperature (10-20.degree. C). The results for the separation of lysyl endopeptidase peptides of globin from Hb solutions made with Hb-rich and Hb-poor animals, indicated the ratios for the compositions of constituent chans of Hb components to differ. The autoxidation rate at pH 7.2 and 35.degree. C was 0.07/h.
DOI: 10.1016/0306-4565(90)90048-M
Type of Publication: Article
