Synthesis of a Marine Bioadhesive Protein.
Abstract
In an attempt to synthesize analogs of the mussel adhesive protein (i.e (A-K-P-S-Y-Hyp-Hyp-T-Dopa-K)80) using recombinant DNA and enzymatic technologies, two major challenges were faced: 1) How to prevent extensive recombination of inserted highly repeated gene sequences in E. coli and Saccharomyces cerevise, and 2) How to bring abour efficient enzymatic hydroxylation of tyrosyl and prolyl residues in expressed analogs. Researchers at Genex Corporation have succeeded in cloning and expressing translation of mussel adhesive anlogs. These contain essentially 20 tandem repeats of the decapeptide excepting 3 T-P-A linkers. Peptide tyrosyl hydroxylation was achieved using mushroom polyphenoloxidase in the presence of ascorbate (BBA (1986) 872, 98). Overall conversion of tyrosine to dopa in the 20-mer was 40-50%. Prolyl hydroxylase has been partially purified from mussel tissue and characterized with respect to substrate specificity.
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 21, 1986
- Accession Number
- ADA175000
Entities
People
- J. H. Waite
Organizations
- University of Delaware