Fish hemoglobins
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/06/2007
|
Resumo |
Vertebrate hemoglobin, contained in erythrocytes, is a globular protein with a quaternary structure composed of 4 globin chains (2 alpha and 2 beta) and a prosthetic group named heme bound to each one. Having myoglobin as an ancestor, hemoglobin acquired the capacity to respond to chemical stimuli that modulate its function according to tissue requirements for oxygen. Fish are generally submitted to spatial and temporal O2 variations and have developed anatomical, physiological and biochemical strategies to adapt to the changing environmental gas availability. Structurally, most fish hemoglobins are tetrameric; however, those from some species such as lamprey and hagfish dissociate, being monomeric when oxygenated and oligomeric when deoxygenated. Fish blood frequently possesses several hemoglobins; the primary origin of this finding lies in the polymorphism that occurs in the globin loci, an aspect that may occasionally confer advantages to its carriers or even be a harmless evolutionary remnant. on the other hand, the functional properties exhibit different behaviors, ranging from a total absence of responses to allosteric regulation to drastic ones, such as the Root effect. |
Formato |
769-778 |
Identificador |
http://dx.doi.org/10.1590/S0100-879X2007000600004 Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 40, n. 6, p. 769-778, 2007. 0100-879X http://hdl.handle.net/11449/22287 10.1590/S0100-879X2007000600004 S0100-879X2007000600004 S0100-879X2007000600004.pdf |
Idioma(s) |
eng |
Publicador |
Associação Brasileira de Divulgação Científica (ABRADIC) |
Relação |
Brazilian Journal of Medical and Biological Research |
Direitos |
openAccess |
Palavras-Chave | #Hemoglobin S #Fish #Root effect #Bohr effect |
Tipo |
info:eu-repo/semantics/article |