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Cloning and Expression of a Synthetic Mussel Adhesive Protein in Escherichia Coli

Published online by Cambridge University Press:  15 February 2011

Anthony J. Salerno
Affiliation:
Allied-Signal Inc., 101 Columbia Road, Morristown, NJ 07962.
Ina Goldberg
Affiliation:
Allied-Signal Inc., 101 Columbia Road, Morristown, NJ 07962.
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Abstract

Repetitious gene cassettes that encode the consensus decapeptide repeat of Mytilus edulis bioadhesive protein were cloned and expressed in Escherichia coli. The bioadhesive precursor (BP, Mx−25,000) was expressed from one 600-bp gene comprised of a 30-bp unit repeat. The repetitious gene appeared stable in a T7-based host/vector system.

Using the T7 expression system for induction, BP was produced at levels approaching 60% of total cell protein. BP was found both in intracellular inclusions and in the soluble fraction. Interestingly, methionine was processed from the N-terminus of the purified protein to give an authentic consensus precursor protein.

Type
Research Article
Copyright
Copyright © Materials Research Society 1993

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