Elsevier

Matrix Biology

Volume 16, Issue 5, November 1997, Pages 245-253
Matrix Biology

Regular papers
A recombinant homotrimer of type I procollagen that lacks the central two D-periods. The thermal stability of the triple helix is decreased by 2 to 4 °C

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Abstract

A D-period cassette system was developed that can be used to synthesize a variety of recombinant homotrimers of type I procollagen. A construct lacking the central two D-periods of proα1(I) chains was assembled and expressed as a recombinant protein in the mammalian cell line. The recombinant protein was purified to homogeneity and the thermal stability of the triple helix assayed by rapid protease digestion. The results indicated that deletion of the central 468 amino acids from the major triple helix lowered the thermal stability of the protein by 2 to 4 °C. The results therefore begin to define regions of the molecule that vary in their contributions to helical stability.

Cited by (0)

1

Present address: Department of Neuroscience, Institute of Neurological Sciences, University of Pennsylvania, Philadelphia, PA 19104.

2

Present address: Center for Gene Therapy, Allegheny University of the Health Sciences, Philadelphia, PA 19102.

3

Present address: Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201.

Copyright © 1997 Published by Elsevier B.V.