The structure of annelid and mollusc hemoglobins.
The polypeptide chain composition and the chemical properties of several annelid hemoglobins and chlorocruorins are presented. In agreement with earlier studies on the hemoglobin from Arenicola cristata (Waxman, L. (1971) J. Biol. Chem. 246, 7318-7327), nearly all of the pigments which have been examined consist of one or more different disulfide-linked polypeptide chains of 13,000 to 16,000 daltons, and the heme-protein stoichiometry suggests that more than one polypeptide is associated with each heme. Except for the prosthetic group, there is no outstanding chemical difference between the chlorocruorins and the hemoglobins, nor is ther any apparent differnce between those hemoglobins which show cooperative oxygen binding properties and those which do not. The results suggest that all these hemoglobins have similar structures. On the other hand, the polypeptide chains of mollusc hemoglobins have molecular weights of greater than 220,000. Each polypeptide binds many heme groups. Thus, annelids use small polypeptide chains while molluscs use giant polypeptides to carry O2.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000845:Annelida / Q000032:analysis*; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007865:Leeches / Q000032:analysis; D008970:Molecular Weight; D008974:Mollusca / Q000032:analysis*; D009835:Oligochaeta / Q000032:analysis; D010100:Oxygen; D010313:Partial Pressure; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides; D011077:Polychaeta / Q000032:analysis; D011485:Protein Binding; D013045:Species Specificity; D013696:Temperature; D014357:Trypsin
D000596:Amino Acids; D006454:Hemoglobins; D010446:Peptide Fragments; D010455:Peptides; D014357:Trypsin; D010100:Oxygen