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  • Title: Two-dimensional electrophoresis of Arenicola marina extracellular hemoglobin: separation of chains with identical molecular mass but different isoelectric point.
    Author: Slitine FE, Toulmond A.
    Journal: Comp Biochem Physiol B; 1991; 100(3):631-4. PubMed ID: 1814687.
    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.
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