Skip to main content

Rattlesnake Hemoglobins: Functional Properties and Tetrameric Stability

Buy Article:

$55.00 plus tax (Refund Policy)

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.





No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Hemoglobin; rattlesnake; tetramer stability

Document Type: Research Article

Affiliations: Depto. de Quimica e Ciencias Ambientais, IBILCE-UNESP, Rua Cristovao Colombo 2265, S.J. do Rio Preto SP, Brazil CEP 15054-000, Brazil.

Publication date: 2006-05-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more