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Synthesis of a Collagen Analog in Escherichia Coli Using Recombinant DNA Technology

Published online by Cambridge University Press:  21 February 2011

Ina Goldberg  and
A. J. Salerno
Ina Goldberg
Affiliation:
Allied-Signal, Inc., Columbia Turnpike, Morristown, NJ 07962
A. J. Salerno
Affiliation:
Allied-Signal, Inc., Columbia Turnpike, Morristown, NJ 07962
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Abstract

A family of totally synthetic genes coding for multiple tandem repeats of the amino acid sequence (Gly-Pro-Pro) has been prepared and inserted into the Clal cloning site of the expression vector pJL6. A representative recombinant plasmid, pACI, with an insert of about 340 bp, was established in an Escherichia coli strain bearing a defective λ prophage, to study expression of the CII-collagen analog fusion protein produced from pACI upon heat induction. The in vivo levels of synthetic gene expression obtained showed that the fusion protein was synthesized in E. coli, but was labile compared to other cellular proteins. This degradation could be significantly reduced by the genetic inhibition of a bacterial protease system.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 174: Symposium R – Materials Synthesis Utilizing Biological Processes , 1989 , 229
Copyright
Copyright © Materials Research Society 1990

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