Internalization of serratial protease into cells as an enzyme-inhibitor complex with alpha 2-macroglobulin and regeneration of protease activity and cytotoxicity.
Open Access
- 1 August 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (23), 10946-10950
- https://doi.org/10.1016/s0021-9258(18)60908-1
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Unusual properties of crocodilian ovomacroglobulin shown in its methylamine treatment and sulfhydryl titrationArchives of Biochemistry and Biophysics, 1986
- Structural changes in alpha-2- and ovomacroglobulins studied by gel chromatography and electron microscopyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Mechanism of .alpha.2-macroglobulin-proteinase interactions. Studies with trypsin and plasminBiochemistry, 1984
- Changes in the binding of "fast"-form .alpha.2-macroglobulin to 3T3-L1 cells after differentiation to adipocytesBiochemistry, 1984
- STUDIES ON THE PHYSIOLOGY OF MACROPHAGE RECEPTORS FOR α‐MACROGLOBULIN · PROTEASE COMPLEXESaAnnals of the New York Academy of Sciences, 1983
- α2‐MACROGLOBULIN: AN INTRODUCTIONAnnals of the New York Academy of Sciences, 1983
- Characterization of functional human .alpha.2-macroglobulin half-molecules isolated by limited reduction with dithiothreitolBiochemistry, 1983
- Rapid acidification of endocytic vesicles containing α2-macroglobulinCell, 1982
- Assay of proteolytic enzymes by the fluorescence polarization techniqueAnalytical Biochemistry, 1979
- Macroglobulin from Human Plasma Which Forms an Enzymatically Active Compound with TrypsinScience, 1964