Expression of a functional alpha-macroglobulin receptor binding domain in Escherichia coli.

Journal Article (Journal Article)

We have expressed receptor-binding domains of human alpha 2-macroglobulin and rat alpha 1-macroglobulin in Escherichia coli. Expression levels of both recombinants were quite high, but the human one was insoluble, probably forming inclusion bodies. The rat domain, which lacks the human disulfide, was produced in a soluble form and readily purified by two simple chromatographic steps. Purified recombinant rat alpha 1-macroglobulin receptor-binding domain was fully functional in binding to the alpha-macroglobulin receptor on human fibroblasts. This 142 residue domain should serve as an excellent template for analyzing the structural requirements for alpha-macroglobulin receptor ligation and dissecting the varied biological functions resulting from such ligation.

Full Text

Duke Authors

Cited Authors

  • Salvesen, G; Quan, LT; Enghild, JJ; Snipas, S; Fey, GH; Pizzo, SV

Published Date

  • November 23, 1992

Published In

Volume / Issue

  • 313 / 2

Start / End Page

  • 198 - 202

PubMed ID

  • 1385222

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(92)81443-p


  • eng

Conference Location

  • England