Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 313 (2), 198-202

Expression of a Functional Alpha-Macroglobulin Receptor Binding Domain in Escherichia Coli

Affiliations

Expression of a Functional Alpha-Macroglobulin Receptor Binding Domain in Escherichia Coli

G Salvesen et al. FEBS Lett.

Abstract

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.

Similar articles

See all similar articles

Cited by 2 articles

Publication types

Substances

LinkOut - more resources

Feedback