Enzymatic properties of α2-macroglobulin-proteinase complexes
- 1 September 1983
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 747 (3), 263-275
- https://doi.org/10.1016/0167-4838(83)90105-x
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Primary and secondary cleavage sites in the bait region of α2‐macroglobulinFEBS Letters, 1981
- Trypsin‐induced activation of the thiol esters in α2‐macroglobulin generates a short‐lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activityFEBS Letters, 1981
- Mechanism of proteinase complex formation with α2‐macroglobulinFEBS Letters, 1981
- Primary structure of the ‘bait’ region for proteinases in α2‐macroglobulinFEBS Letters, 1981
- Proteolytic cleavage sites on α2-macroglobulin resulting in proteinase binding are different for trypsin and staphylococcus aureus V-8 proteinaseBiochemical and Biophysical Research Communications, 1981
- Sequence location of the reactive thiol ester in human α2 -macroglobulinFEBS Letters, 1981
- A thiol‐ester in α2‐macroglobulin cleaved during proteinase complex formationFEBS Letters, 1980
- The influence of α2‐macroglobulin on the elastolytic and esterolytic activity of elastaseFEBS Letters, 1970
- On the Determination of Molar Concentration of Plasmin and Plasmin Inhibitors.Acta Chemica Scandinavica, 1967
- The Combining Ratio between Trypsin and Serum alpha2-Macroglobulin.Acta Chemica Scandinavica, 1966