Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/96002
Type: Artigo de periódico
Title: Oxygenation Properties Of Hemoglobin From The Turtle Geochelone Carbonaria.
Author: Torsoni M.A.
Ogo S.H.
Abstract: The oxygen-binding properties of hemoglobin (Hb) from the adult terrestrial turtle Geochelone carbonaria are described. Turtle hemoglobins have a low intrinsic oxygen affinity and a low sensitivity to an endogenous cofactor (ATP) usually present at high concentrations in the reptile erythrocytes. The amplitude of the Bohr effect for O2 binding was virtually the same in the absence and presence of saturating ATP concentrations (delta logP50/delta pH, about -0.60) and increased in the total hemolysate (-0.83). The large Bohr effect found in G. carbonaria Hb may be important for O2 delivery to the tissue. The degree of cooperativity displayed by Hb for O2 binding ranged between 1.5 and 2.0 in stripped solution and total hemolysate. These observations suggest that stability of the low affinity conformation, which needs to be confirmed by additional experiments.
Editor: 
Rights: aberto
Identifier DOI: 
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0029398408&partnerID=40&md5=16884c57ef3391b4090cff963e7cea08
Date Issue: 1995
Appears in Collections:Unicamp - Artigos e Outros Documentos

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