The Primary Structure of the Hemoglobin of the Brazilian Manatee (Trichechus inunguis, Sirenia)

Abstract

The hemoglobin of the Brazilian Manatee {Trichechus inunguis, Sirenia) consists of one component. We present the primary structures of the α- and β-chains which have been separated by chromatography on carboxy-methyl-cellulose Cm-Kresol52. The sequences have been determined by automatic Edman degradation with the film technique, using the native chains, tryptic peptides and the C-terminal prolyl-peptide obtained by acid hydrolysis of the Asp-Pro bond of the α-chains.Compared to the corresponding human chains we found 27 substitutions in the α- as well as in the ß-chains. Three heme contacts and four α1 /β1 contacts between the subunits are affected by exchanges.The hemoglobin of Trichechus inunguis is compared with those of Elephas maximus, Loxodonta africana, and Procavia habessinica and the monophyletic origin of the superorder Paenungulata is discussed. © 1988, Walter de Gruyter. All rights reserved.