The primary structure of globin and linker chains from the chlorocruorin of the polychaete Sabella spallanzanii
Pallavicini, A.; Negrisolo, E.; Barbato, R.; Dewilde, S.; Ghiretti-Magaldi, A.; Moens, L.; Lanfranchi, G. (2001). The primary structure of globin and linker chains from the chlorocruorin of the polychaete Sabella spallanzanii. J. Biol. Chem. 276(28): 26384-26390. https://dx.doi.org/10.1074/jbc.M006939200
In: Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology: Baltimore, etc.. ISSN 0021-9258; e-ISSN 1083-351X, more
Annelid hemoglobins are organized in a very complex supramolecular network of interacting polypeptides, the structure of which is still not wholly resolved. We have separated by two-dimensional electrophoresis the 4-MDa chlorocruorin ofSabella spallanzanii and identified its components by amino-terminal sequencing. This work reveals a high rate of heterogeneity of constituent chains in a single animal as well as in the Sabella population. Using a cDNA library prepared from the hematopoietic tissue of this worm, we have isolated and fully sequenced most globin and linker cDNAs. The primary structure features of these polypeptides have been characterized by comparison with model globin and linker sequences.
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