Abstract
The present work analyzed the tetrameric stability of the hemoglobins from the rattlesnake C. durissus terrificus using analytical gel filtration chromatography, SAXS and osmotic stress. We show that the dissociation mechanism proposed for L. miliaris hemoglobin does not apply for these hemoglobins, which constitute stable tetramers even at low concentrations.
Keywords: Hemoglobin, rattlesnake, tetramer stability
Protein & Peptide Letters
Title: Rattlesnake Hemoglobins: Functional Properties and Tetrameric Stability
Volume: 13 Issue: 5
Author(s): Fabio R. Lombardi, Maristella C. Anazetti, Giovanni C. Santos, Johnny R. Olivieri, Walter F. de Azevedo Jr. and Gustavo O. Bonilla-Rodriguez
Affiliation:
Keywords: Hemoglobin, rattlesnake, tetramer stability
Abstract: The present work analyzed the tetrameric stability of the hemoglobins from the rattlesnake C. durissus terrificus using analytical gel filtration chromatography, SAXS and osmotic stress. We show that the dissociation mechanism proposed for L. miliaris hemoglobin does not apply for these hemoglobins, which constitute stable tetramers even at low concentrations.
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Cite this article as:
Lombardi R. Fabio, Anazetti C. Maristella, Santos C. Giovanni, Olivieri R. Johnny, de Azevedo Jr. F. Walter and Bonilla-Rodriguez O. Gustavo, Rattlesnake Hemoglobins: Functional Properties and Tetrameric Stability, Protein & Peptide Letters 2006; 13 (5) . https://dx.doi.org/10.2174/092986606776819484
DOI https://dx.doi.org/10.2174/092986606776819484 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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