Characterisation of the Adhesive Proteins of a Major Fouling Organism, the Barnacle
Abstract
Solidified adhesive (cement) of the balanid barnacle, Balanus crenatus (Crustacea: Cirripedia) was dissolved using sodium dodecyl sulphate with and without the addition of the reducing agent, 2-mercaptoethanol. The protein(s) which makes up the cement is heat sensitive demonstrating its hydrophobic nature. Other problems with the dissolution of the cement are due to the abundant sulphur cross-links which appear to be buried in hydrophobic cores and are inaccessible to the reductant. Dissolution of the cement was achieved by grinding the wet cement in water to produce a fine suspension, adding a buffer with SDS (4 %) and allowing to stand at no higher than 60 *C for a minimum of 30 min. (optimum temperature = 40 deg C). Non-reducing SDS-PAGE revealed numerous bands ranging in size from 2 to-46 kD which were reduced to a minimum of 2 bands of roughly 2.5 and 3 kD. These proteins were blotted from SDSPAGE tricine gels onto polyvinylidene difluoride membrane for modification, amino acid analysis and sequencing.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 15, 1993
- Accession Number
- ADA269941
Entities
People
- Michael J. Naldrett
Organizations
- University of Reading