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|Type:||Artigo de periódico|
|Title:||Oxygen-binding properties of total hemoglobin and isolated components of the terrestrial tortoise Geochelone carbonaria|
|Abstract:||The hemoglobin of the terrestrial tortoise Geochelone carbonaria was separated into two major components by ion exchange chromatography. The oxygen binding properties of both the unfractionated hemolysate and the separated components were investigated. The stripped hemoglobin of G. carbonaria displayed an oxygen affinity of approximately 6.3 mm Hg at pH 7.4 with a Bohr effect of about -0.55. The Hb-O-2 binding properties were also studied in the presence of the organic polyphosphates ATP and IHP. Inositol hexaphosphate (IHP) was more effective in lowering oxygen affinity, yielding a P-50 Of 20.1 mm Hg at pH 7.4. The n(50) value were quite low in the stripped form of the protein (1.0-1.9) but increased in the presence of both organic phosphates, attaining a value of approximately 2.9 at pH 7.9. The oxygen binding properties of the major hemo globin components were also investigated in the presence and absence of organic phosphates, and the values were compared with those obtained for the total hemolysate. (C) 1997 Elsevier Science Inc.|
|Editor:||Pergamon-elsevier Science Ltd|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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