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Fish hemoglobins BJMBR
Souza,P.C. de; Bonilla-Rodriguez,G.O..
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...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Hemoglobins; Fish; Root effect; Bohr effect.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007000600004
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Functional properties of the three hemoglobin phenotypes of Nelore cattle Genet. Mol. Biol.
Di Vito,A.; Schwantes,A.R.; Schwantes,M.L.B..
Blood and stripped hemoglobin from Nelore cattle individuals were submitted to oxygen equilibrium experiments in both gasometric and spectrophotometric methods. No difference was detected in oxygen affinity and Bohr effect among Hb A, Hb B and Hb AB in experiments with both blood and stripped hemoglobin, in the presence and absence of the chloride ion. However, n values (Hill plots) were higher in Hb B and Hb AB (>2) than in Hb A (<2).
Tipo: Info:eu-repo/semantics/article Palavras-chave: Allohemoglobins; Functional properties; Nelore cattle; Cooperativity; Bohr effect; Modulatators effect.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572002000200004
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