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Involvement of available SH groups in the heterogeneity of hemoglobin from the tortoise Geochelone carbonaria
Author(s) -
Torsoni M. A.,
SouzaTorsoni A.,
Ogo S. H.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201902
Subject(s) - iodoacetamide , hemoglobin , chromatography , size exclusion chromatography , polyacrylamide gel electrophoresis , chemistry , electrophoresis , globin , cellulose , biochemistry , cysteine , enzyme
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 fresh 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 (G1, G2 and G3). Both Hb components shared the G1 globin chain with HbI containing G1 and G2 and HbII, G1 and G3 chains.