Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Binding, Competitive
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Humans
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Low Density Lipoprotein Receptor-Related Protein-1
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Methylamines / metabolism
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Methylamines / pharmacology
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Folding
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Rats
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Receptors, Immunologic / metabolism*
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Recombinant Proteins / chemistry
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Sequence Alignment
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alpha-Macroglobulins / chemistry*
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alpha-Macroglobulins / genetics*
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alpha-Macroglobulins / metabolism
Substances
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Low Density Lipoprotein Receptor-Related Protein-1
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Methylamines
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Peptide Fragments
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Receptors, Immunologic
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Recombinant Proteins
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alpha-Macroglobulins
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methylamine