Expression and refolding of a high-affinity receptor binding domain from rat alpha 1-macroglobulin.
A recombinant version of the receptor binding domain of rat alpha 1-macroglobulin (RBDv) consisting of residues 1319-1474 has been expressed in E. coli. Competition experiments with 125I-labelled methylamine treated human alpha 2-macroglobulin reveal that the alpha 1-macroglobulin-RBDv exhibit the same high affinity for the alpha 2-macroglobulin receptor as the entire 40 kDa light chain from rat alpha 1-macroglobulin. It is therefore concluded, that all determinants for receptor interaction reside in the C-terminal approx. 150 residues of the alpha-macroglobulin subunit.
Nielsen
K L
KL
Department of Chemistry, University of Arhus, Denmark.
Sottrup-Jensen
L
L
Fey
G H
GH
Thøgersen
H C
HC
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D006801:Humans; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D008744:Methylamines / Q000378:metabolism / Q000494:pharmacology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D051381:Rats; D011971:Receptors, Immunologic / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
D026503:Low Density Lipoprotein Receptor-Related Protein-1; D008744:Methylamines; D010446:Peptide Fragments; D011971:Receptors, Immunologic; D011994:Recombinant Proteins; D000511:alpha-Macroglobulins; C027451:methylamine