Rattlesnake hemoglobins: Functional properties and tetrameric stability.
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.
Lombardi
Fabio Renato
FR
Depto. de Química e Ciências Ambientais, IBILCE-UNESP, Rua Cristóvão Colombo 2265, S.J. do Rio Preto SP, Brazil CEP 15054-000.
Anazetti
Maristella Conte
MC
Santos
Giovanni César
GC
Olivieri
Johnny Rizzieri
JR
de Azevedo
Walter Filgueira
WF
Bonilla-Rodriguez
Gustavo Orlando
GO
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D017839:Crotalus; D006454:Hemoglobins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008433:Mathematics; D010100:Oxygen / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary
D006454:Hemoglobins; D000255:Adenosine Triphosphate; D010100:Oxygen