The primary structure of globin and linker chains from the chlorocruorin of the polychaete Sabella spallanzanii.
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 of Sabella 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.
Pallavicini
A
A
Dipartimento di Biologia and Centro di Ricera Interdipartimentale per le Biotechnologie Innovative Biotechnology Center, Università di Padova, Via Ugo Bassi 58/B, 35131 Padova, Italy.
Negrisolo
E
E
Barbato
R
R
Dewilde
S
S
Ghiretti-Magaldi
A
A
Moens
L
L
Lanfranchi
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D005914:Globins / Q000737:chemistry / Q000235:genetics*; D006420:Hemeproteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D011077:Polychaeta; D016415:Sequence Alignment
D018076:DNA, Complementary; D006420:Hemeproteins; C010884:chlorocruorin; D005914:Globins