Hemoglobin-binding proteins in the amphibian Taricha granulosa Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/f4752m23h

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  • The first reported observation of hemoglobin association with a plasma protein was made by Polonovski and Jayle in 1938. Since that time, countless investigators have contributed to the characterization of the hemoglobin- binding plasma protein, haptoglobin. Haptoglobins have been found in many mammals, including humans and in various birds. However, very little research has been applied to reptilian and amphibian systems regarding haptoglobin presence. This study investigated the amphibian Taricha granulosa with regard to the presence of haptoglobin in its plasma and the overall ability of the animal to exhibit hemoglobin conservation upon hemolysis. Results of this research indicated that although the newt is void of haptoglobin, it is capable of binding free hemoglobin and demonstrates hemoglobin and iron conservation upon induced hemolysis. In vitro experiments suggested that two serum albumins as well as a slightly larger plasma glycoprotein associate with free hemoglobin in the newt. The stoichiometry of interaction of the albumins to hemoglobin or the glycoprotein to hemoglobin is apparently one hemoglobin-αβ binding protein to one-half hemoglobin (one as dimer). The hemoglobin of the newt was also observed to lack affinity for human haptoglobin.. Since bacteriostasis has been suggested to be another function of haptoglobin, the hemoglobin-plasma protein complexes of Taricha along with the complex of mouse hemoglobin-human haptoglobin were used to supplement growth media for culturing two species of β-hemolytic bacteria. In each case, the bacteria were able to acquire the radiolabeled heme iron from the complexes as easily as from the respective free hemoglobins.
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