The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG1. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.
|ジャーナル||Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular|
|出版ステータス||Published - 1986 12 12|
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