Separation of free and chymotrypsin-bound alpha 2-macroglobulin by affinity chromatography. Its use to demonstrate that the two chymotrypsin-binding sites of alpha 2-macroglobulin are equivalent and independent.
Open Access
- 1 June 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (12) , 6683-6685
- https://doi.org/10.1016/s0021-9258(18)34483-1
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Primary structure of the ‘bait’ region for proteinases in α2‐macroglobulinFEBS Letters, 1981
- Human pancreatic cationic trypsin as a possible mediator of pancreatic shock as inferred from a study of its interaction with serum and α2-macroglobulinBiochemical Medicine, 1977
- On the inhibition of elastase by serum. Some distinguishing properties of α1-antitrypsin and α2-macroglobulinClinica Chimica Acta; International Journal of Clinical Chemistry, 1975
- Modifications structurales de l'α1-macroglobuline de rat par la fixation d'enzymes proteolytiques mise en evidence par electrophorése et microscopie électroniqueInternational Journal of Biochemistry, 1975
- Degradation of Human Fibrinogen by Plasma α2-Macroglobulin-Enzyme ComplexesJournal of Clinical Investigation, 1973
- Thiol reduction of human α2-macroglobulin. The subunit structureBiochemical Journal, 1972
- The separation of alpha-2 macroglobulin into five components with differing electrophoretic and enzyme-binding propertiesJournal of Clinical Investigation, 1971
- The influence of α2‐macroglobulin on the elastolytic and esterolytic activity of elastaseFEBS Letters, 1970
- Selective enzyme purification by affinity chromatography.Proceedings of the National Academy of Sciences, 1968
- The action of chymotrypsin on two new chromogenic substratesArchives of Biochemistry and Biophysics, 1966