GENERATION AND REACTIVITY OF "NASCENT" ?2-MACROGLOBULIN: LOCALIZATION OF CROSS-LINKS IN ?2-MACROGLOBULIN-TRYPSIN COMPLEX
- 1 December 1983
- journal article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 421 (1 Chemistr) , 188-208
- https://doi.org/10.1111/j.1749-6632.1983.tb18109.x
Abstract
No abstract availableThis publication has 29 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
- Further characterization of the covalent linking reaction of α2-macroglobulinBiochemical Journal, 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
- Reactive site in human alpha 2-macroglobulin: circumstantial evidence for a thiolester.Proceedings of the National Academy of Sciences, 1981
- A thiol‐ester in α2‐macroglobulin cleaved during proteinase complex formationFEBS Letters, 1980
- Determination of α2-macroglobulin as trypsin-protein esteraseClinica Chimica Acta; International Journal of Clinical Chemistry, 1966
- Macroglobulin from Human Plasma Which Forms an Enzymatically Active Compound with TrypsinScience, 1964