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Over-Expression of a Core Repeat from an Insect Silk Protein that forms Intramolecular Disulfide Bonds

Published online by Cambridge University Press:  15 February 2011

Stanley V. Smith  and
Steven T. Case
Stanley V. Smith
Affiliation:
Department of Biochemistry, The University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216-4505.
Steven T. Case
Affiliation:
Department of Biochemistry, The University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216-4505.
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Abstract

A gene encoding one complete [C+SR] core repeat from spIa, a 1000-kDa silk protein from Chironomus tentans, was synthesized and its recombinant protein expressed to high levels in bacterial cells. We observed that reducing agents significantly alter the electrophoretic mobility of this protein. A variety of data indicate that the purified recombinant protein is folded and its structure stabilized by two intramolecular disulfide bonds.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 292: Symposium S – Biomolecular Materials , 1992 , 93
Copyright
Copyright © Materials Research Society 1993

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References

1. Case, S.T. and Wieslander, L., in Results and Problems in Cell Differentiation, edited by Case, S.T. (Springer-Verlag, Berlin Heidelberg, 1992) p. 187.Google Scholar
2. Wellman, S.E. and Case, S.T., J. Biol. Chem. 264, 10878 (1989).Google Scholar
3. Wellman, S.E., Hamodrakas, S.J., Kamitsos, E.I. and Case, S.T., Biochim. Biophys. Acta 1121, 279 (1992).Google Scholar
4. Tirrell, D.A., Fournier, M.J., and Mason, T.L., Mater. Res. Bull. 16 (7), 23 (1991).Google Scholar
5. Mullis, K.B. and Faloona, F.A., Methods Enzymol. 155, 335 (1987).Google Scholar
6. Studier, F.W., Rosenberg, A.H., Dunn, J.D. and Dubendorff, J.W., Methods Enzymol. 185, 60 (1990).Google Scholar
7. Ellman, G.L., Arch. Biochem. Biophys. 82, 70 (1959).Google Scholar
8. Hamodrakas, S.J. and Kafatos, F.C., J. Mol. Evol. 20, 296 (1984).Google Scholar
9. Hwang, C., Sinskey, A.J., and Lodish, H.F., Science 257, 1496 (1992).Google Scholar