Abstract
1. 1. Vertical starch-gel electrophoresis at pH 8.6 revealed specific hemoglobin multiplicity in most hemoglobin hemolysates isolated from 13 Gulf of Mexico fish species. 2. 2. All hemoglobins isolated are tetramers based upon gel filtration chromatography. 3. 3. Isothermal denaturation in the presence of urea indicates large differences in the denaturation and unfolding behavior at 25°C. 4. 4. Significant Root effects were observed below pH 7.0 for individual hemoglobin components of menhaden, Brevoortia patronus, and the striped bass, Morone saxatilis. 5. 5. Large differences in the rate of autoxidation were determined for many of the hemoglobins examined. 6. 6. Two species of catfish, Arius felis and Bagre marinus, possessed the most stable hemoglobins and lowest rate of autoxidation compared to the other species of fish studied.
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