[The primary structure of hemoglobin from goldfish (Carassius auratus)].
The primary structures of the alpha- and beta-chains from goldfish hemoglobin are given. The globin chains were separated by gel filtration after air-oxidation of globin. After chemical and enzymatical cleavage of the chains, the peptides were isolated by gel filtration and ion exchange chromatography on Dowex. The fish-chains have one residue more than the human chains. The alpha-chain is acetylated at the amino-terminal residue and has no cysteine. Compared with the human chains there are 66 amino-acid differences in the alpha- and 72 in the beta-chains. The implication of these differences for the physiology of the hemoglobin molecule of goldfish is discussed.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D003530:Cyprinidae / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D006054:Goldfish / Q000097:blood*; D006454:Hemoglobins / Q000302:isolation & purification*; D006868:Hydrolysis; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D006454:Hemoglobins; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin
Die Primärstruktur des Hämoglobins vom Goldfisch (Carassius auratus).