PRIMARY STRUCTURE OF HEMOCYANIN SUBUNIT-C FROM PANULIRUS-INTERRUPTUS

B NEUTEBOOM, PA JEKEL, JJ BEINTEMA

    Research output: Contribution to journalArticleAcademicpeer-review

    42 Citations (Scopus)

    Abstract

    The amino acid sequence of the hemocyanin subunit c from the spiny lobster, Panulirus interruptus, has been determined. The elucidation was mainly based on three digests, with CNBr, trypsin and endoproteinase Glu-C, respectively. Additional evidence was obtained by sequencing of peptides from an endoproteinase Lys-C digest. Subunit c is a polypeptide with 661 amino acid residues and' with a carbohydrate group attached to residue 476 in the third domain. No heterogeneity was observed. The degree of identity with subunit a is 59%. Some differences with subunit a are an N-terminal extension of six residues, a one-residue C-terminal extension, and a three-residue deletion. Furthermore, carbohydrate attachment is in a different position, as are most half-cystine residues. Limited trypsinolysis resulted in cleavage at the same site as in subunits a and b.

    Original languageEnglish
    Pages (from-to)243-249
    Number of pages7
    JournalEuropean Journal of Biochemistry
    Volume206
    Issue number1
    Publication statusPublished - 15-May-1992

    Keywords

    • AMINO-ACID-SEQUENCE
    • EURYPELMA-CALIFORNICUM
    • ARTHROPOD HEMOCYANINS
    • LIMITED PROTEOLYSIS
    • DISULFIDE BRIDGES
    • PROTEINS
    • PEPTIDES
    • SPIDERS
    • SITE

    Cite this