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Limited proteolysis of the alpha-macroglobulin rat alpha 1-inhibitor-3. Implications for a domain structure

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  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
Rat alpha 1-inhibitor-3 is a 180-kDa monomeric proteinase inhibitor found in high concentration in rat plasma. By several criteria it has been shown to be a member of the family of alpha-macroglobulin proteinase inhibitors often exemplified by the tetrameric human alpha 2-macroglobulin. We have used limited proteolysis of rat alpha 1-inhibitor-3 to probe the domain structure of this family of proteins. Proteinases of different specificities, including trypsin, chymotrypsin, thermolysin, and Staphylococcus aureus V8 proteinase, were employed and a common fragmentation pattern was observed when the reaction products were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These fragments were electrotransferred to polyvinylidene difluoride membranes and subjected to NH2-terminal amino acid sequence analysis in order to position them within the context of the primary structure. The fragmentation pattern may define the domain structure of alpha 1-inhibitor-3 and serve as a model for the domain organization of the family of alpha-macroglobulin proteinase inhibitors.
Original languageEnglish
JournalJournal of Biological Chemistry
Pages (from-to)11252-61
Number of pages9
Publication statusPublished - 1991

    Research areas

  • Acute-Phase Proteins, Amino Acid Sequence, Animals, Chymotrypsin, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Molecular Weight, Papain, Peptide Fragments, Peptide Mapping, Protease Inhibitors, Rats, Thermolysin, Trypsin, alpha-Macroglobulins

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