title: Two-dimensional electrophoresis of Arenicola marina extracellular hemoglobin: separation of chains with identical molecular mass but different isoelectric point.
abstract: 1. On the basis of their molecular masses, four types of polypeptides (A, B, C, D) were obtained by SDS-PAGE of the extracellular hemoglobin of the polychaete annelid Arenicola marina. 2. On 2-dimensional polyacrylamide gel electrophoresis, the erythrocruorin dissociated into six different types of polypeptide chains; A1, A2, B1, B2, C and D. 3. A1 and B1 migrate in 2-dimensional electrophoresis at the same position as alpha and beta chains of human hemoglobin.
authors.affiliation: Laboratoire de Biologie et Physiologie marines, Université Pierre et Marie Curie, Paris, France.
authors.forename: F E
authors.initials: FE
authors.lastname: Slitine
authors.forename: A
authors.initials: A
authors.lastname: Toulmond
mesh_terms: D000818:Animals; D000845:Annelida; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007526:Isoelectric Point
chemical_list: D006454:Hemoglobins; C064665:erythrocruorin