Identification of the globin chain and the amino acid residue responsible for polymerization of bullfrog (Rana catesbeiana) hemoglobin with iodo[14C]acetamide.
The bullfrog (Rana catesbeiana) major hemoglobin dissociates into its constituent globin chains (alpha and beta) which are separated by Sulfopropyl-Sephadex C-25 column chromatography after alkylation with iodo[14C]acetamide. Each globin chain has two cysteine residues and those of the beta-globin chain in the tetramer are preferentially alkylated with iodoacetamide.
D000818:Animals; D001001:Anura; D003545:Cysteine; D005914:Globins; D006454:Hemoglobins; D007460:Iodoacetamide; D007461:Iodoacetates; D046911:Macromolecular Substances; D011485:Protein Binding; D011892:Rana catesbeiana
D006454:Hemoglobins; D007461:Iodoacetates; D046911:Macromolecular Substances; D005914:Globins; D003545:Cysteine; D007460:Iodoacetamide