title: Preparation and chemical characterization of the three chains of the major hemoglobin of the sea snake, Pelamis platurus.
abstract: One of the 2 main hemoglobins of the sea snake Pelamis platurus, (the Yellow-bellied sea snake) comprising about 70% of the total hemoglobin, was separated by DEAE-Sephadex column chromatography. From results of gel filtration and iron content determination, both intact sea snake hemoglobin, and the isolated major hemoglobin, were concluded to be composed of 4 subunits with a molecular weight of 66,000-67,000 daltons. Separation of the chains of globin of the major hemoglobin by CM 52 column chromatography gave 3 peaks, named, chains a, b, and c. The approximate molecular weights of chains a, b, and c were deduced by SDS gel electrophoresis to be 14,000, 16,000, and 20,000 daltons, respectively. The peptide maps  and amino acid compositions of the three chains were distinctly different. N-Terminal and C-terminal amino acid sequence studies reveal that chains a, b, and c represented the alpha-chain, beta-chain, and beta'-chain differing from the normal beta-chain in having a C-terminal sequence of -Arg-Leu-His-Tyr. From the peak areas of the 3 chains obtained by CM 52 column chromatography, and the peak sizes of the 3 bands separated by SDS gel electrophoresis, it was concluded that the sea snake hemoglobin is composed of a hybrid tetramer, alpha2betabeta'.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002263:Carboxyhemoglobin / Q000032:analysis; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis*; D007501:Iron / Q000032:analysis; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D012911:Snakes / Q000097:blood*
chemical_list: D000596:Amino Acids; D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D002263:Carboxyhemoglobin; D007501:Iron