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|Type:||Artigo de periódico|
|Title:||Involvement of available SH groups in the heterogeneity of hemoglobin from the tortoise Geochelone carbonaria|
|Abstract:||Geochelone carbonaria hemoglobin (Hb) was analyzed by polyacrylamide gel electrophoresis (PAGE) and purified by ion exchange chromatography on CM-cellulose. Seven fractions were obtained using flesh Hb preparations. CM-cellulose chromatography of Hb reacted with iodoacetamide, showed one minor (HbI) and one major band (HbII). Analysis of the molecular masses of recently collected Hb and of aged solutions determined by gel filtration showed that polymerization increased with the duration of storage. The reaction with oxidized glutathione changed the electrophoretic pattern of Hb, and highlighted the bands corresponding to glutathionyl-Hb. The presence of these bands in fresh Hb solutions and in alkylated preparations suggests that they may occur in vivo. PAGE under dissociating conditions showed that the hemolysate contained 3 different polypeptide chains (G(1), G(2) and G(3)). Both Hb components shared the G(1) globin chain with HbI containing G(1) and G(2) and HbII, G(1) and G(3) chains.|
|Editor:||Academic Press Aust|
|Citation:||Biochemistry And Molecular Biology International. Academic Press Aust, v. 44, n. 4, n. 851, n. 860, 1998.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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