Hemocyanins in spiders, X. Limited proteolysis of chain e of Eurypelma hemocyanin and partial sequence of two large fragments.
The polypeptide chain e of the homocyanin from the spider Eurypelma californicum was isolated by ion exchange chromatography. Incubation of the undenatured protein with chymotrypsin, subtilisin, or trypsin resulted in a small number of large fragments which were easily isolated after denaturation. Of the chymotryptic peptides e-Chn-29 was found to be N-terminal, and e-Chn-42 C-terminal. These peptides were characterized by their N-terminal amino acid sequences. The N-terminal sequence of subunit e shows homologies with other arthropod hemocyanins.
D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin; D006433:Hemocyanins; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013112:Spiders / Q000032:analysis*; D014357:Trypsin
D046911:Macromolecular Substances; D010446:Peptide Fragments; D006433:Hemocyanins; D002918:Chymotrypsin; D014357:Trypsin