In vitro binding and in vivo clearance of human alpha 2-macroglobulin after reaction with endoproteases from four different classes.

Journal Article (Journal Article)

The binding of human alpha 2-macroglobulin complexed with trypsin, papain, thermolysin and cathepsin-D to murine macrophages was studied at 4 degrees C. Similar dissociation constants (0.4 nM) were determined for all of the complexes except alpha 2-macroglobulin-cathepsin-D (0.7 nM). Radioiodinated alpha 2-macroglobulin-protease complexes were injected into mice, and the clearance studied. Native alpha 2-macroglobulin cleared slowly, as previously reported, while greater than 50% of the complexes formed with trypsin, papain and thermolysin cleared in less than 5 min. The clearance of alpha 2-macroglobulin-cathepsin-D was biphasic, suggesting that only about half the alpha 2-macroglobulin was present in a reacted complex.

Full Text

Duke Authors

Cited Authors

  • Feldman, SR; Ney, KA; Gonias, SL; Pizzo, SV

Published Date

  • July 29, 1983

Published In

Volume / Issue

  • 114 / 2

Start / End Page

  • 757 - 762

PubMed ID

  • 6192823

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/0006-291x(83)90845-8


  • eng

Conference Location

  • United States