Alpha 2-macroglobulin-proteinase complexes, plasminogen activator inhibitor type-1-plasminogen activator complexes, and receptor-associated protein bind to a region of the alpha 2-macroglobulin receptor containing a cluster of eight complement-type repeats
| Autor: | Hans Christian Thøgersen, Peter A. Andreasen, Michael Etzerodt, Anders Nykjaer, Lars Sottrup-Jensen, Thor Las Holtet, H. H. Rasmussen, Jørgen Gliemann, S K Moestrup |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
biology Activator (genetics) Cell Biology Ligand (biochemistry) Biochemistry Molecular biology Amino acid LDL-receptor-related protein-associated protein alpha-2-Macroglobulin chemistry biology.protein Binding site Molecular Biology Peptide sequence Plasminogen activator |
| Zdroj: | Moestrup, S K, Holtet, T L, Etzerodt, M, Thøgersen, H C, Nykjær, A, Andreasen, P, Rasmussen, H H, Sottrup-Jensen, L & Gliemann, J 1993, ' Alpha 2-macroglobulin-proteinase complexes, plasminogen activator inhibitor type-1-plasminogen activator complexes, and receptor-associated protein bind to a region of the alpha(2)-Macroglobulin receptor containing a cluster of eight complement-type repeats ', Journal of Biological Chemistry, vol. 268, no. 18, pp. 13691-13696 . |
| ISSN: | 0021-9258 |
| Popis: | A region containing sites for ligand binding was localized in the 4525-amino acid residue alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein (alpha 2MR/LRP) by ligand- and immunoblotting of proteinase and CNBr digests of the purified human placental protein. 125I-Labeled rat alpha 1-macroglobulin light chain, urokinase-plasminogen activator inhibitor type-1 complex, and alpha 2MR-associated protein all bound to a 75-kDa CNBr-generated fragment (68 kDa after deglycosylation). In addition to the three ligands, the fragment bound a novel monoclonal antibody reacting in the region defined by amino acid residues 1165-1246 as determined by binding to recombinant fragments of alpha 2MR/LRP. The positions of methionine residues in alpha 2MR/LRP suggested that the ligand-binding CNBr fragment contained three disulfide-linked peptides comprising the residues 776-1399. This origin was confirmed by partial amino acid sequencing of the electroblotted fragment and polypeptides generated by reduction of the fragment. The identified region represents 13.6% of the molecular mass (nonglycosylated) of alpha 2MR/LRP and contains one of three large clusters of complement-type repeats. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|