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  • Title: Hemocyanins in spiders, X. Limited proteolysis of chain e of Eurypelma hemocyanin and partial sequence of two large fragments.
    Author: Schneider HJ, Schartau W, Linzen B, Lottspeich F, Henschen A.
    Journal: Hoppe Seylers Z Physiol Chem; 1980 Aug; 361(8):1211-6. PubMed ID: 7409754.
    Abstract:
    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.
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