Characterization of barnacle (Balanus eburneus and B. cenatus ) adhesive proteins |
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Authors: | M J Naldrett D L Kaplan |
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Institution: | (1) John Innes Centre, Norwich Research Park, Colney Lane, Colney, Norwich NR4 7UH, United Kingdom, GB;(2) Tufts University, Biotechnology Center, Department of Chemical Engineering, 4 Colby Street, Medford, Massachusetts 02155, USA, US |
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Abstract: | Cements from two species of barnacles, Balanuseburneus Gould and Balanus crenatus Bruguiére, 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 ˜ 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 °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 °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 ˜ 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.
Received: 7 August 1996 / Accepted: 8 October 1996 |
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