Abstract
1. 1. The electrophoretic mobilities of hemoglobins from eleven species of delphinids are compared. 2. 2. Only four hemoglobin arrays are observed in the elecrophoretic study. Each of the species exhibits only one of the four observed hemoglobin complements. 3. 3. The oxygen dissociation curves are presented for each of three hemoglobin complements at various pH values. Comparisons show each of the arrays to have distinct functional properties. Electrophoretically indistinguishable hemoglobin complements were found to have indistinguishable functions in a three species complex indicating probable identity. Another species pair with electrophoretically indistinguishable hemoglobins had disparate O 2 dissociation properties indicating molecular dissimilarity. 4. 4. Bohr factors are shown to vary slightly in the physiological pH range. 5. 5. Concentrations of lactic acid shift the P 50 values very slightly toward dissociation in an effect similar to that described for other salt concentrations. CO 2 concentrations appear to have little effect on oxygen-binding properties at a fixed pH.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Comparative Biochemistry and Physiology -- Part A: Physiology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
