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
Language
- eng
Conference Location
- United States