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Expression of a functional α‐macroglobulin receptor binding domain in Escherichia coli
Author(s) -
Salvesen Guy,
Quan Long T.,
Enghild Jan J.,
Snipas Scott,
Fey Georg H.,
Pizzo Salvatore V.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81443-p
Subject(s) - escherichia coli , macroglobulin , chemistry , microbiology and biotechnology , receptor , domain (mathematical analysis) , computational biology , biology , biochemistry , gene , mathematics , mathematical analysis
We have expressed receptor‐binding domains of human α 2 ‐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 α 1 ‐macroglobulin receptor‐binding domain was fully functional in binding to the α‐macroglobulin receptor on human fibroblasts. This 142 residue domain should serve as an excellent template for analyzing the structural requirements for α‐macroglobulin receptor ligation and dissecting the varied biological functions resulting from such ligation.