Characterization of barnacle (Balanus eburneus and B-cenatus) adhesive proteins

Cements from two species of barnacles, Balanus eburneus could and Balanus crenatus Bruguiere, were analyzed to identify the number and nature of proteins present. B. crenatus cement was composed mainly of a small peptide cross-linked into aggregates ranging in size from similar to 3 kD to 40-50 kD. These aggregates could be reduced with 2-mercaptoethanol (2-ME) in the presence of sodium dodecyl sulfate (SDS) but only after incubation at 40 degrees C for 12 to 24 h and only when the cement was recently formed. Reductive alkylation of cysteine residues with 4-vinylpyridine produced a water-soluble peptide of less than 5 kD. By comparison, the cement of B. eburneus could be dissolved only partially in SDS and 2-ME when heated at 100 degrees C for 10 min. Five major proteins were identified by SDS-PAGE: 7, 22, 36 and 58 kD bands for which N-terminal sequence and amino acid compositions are presented; and a 52 kD band for which sequence data are given. A minor protein band of similar to 80 kD has the same N-terminus as the 36 kD band. CNBr digests of individual proteins produced peptides for which sequence and composition data are also presented. The study was conducted during 1993 to 1995. In general, the proteins identified from B. crenatus cement are similar to those characterized from B. eburneus, and they are different in composition and sequence than those previously reported from Mytilus edulis.