Computer Averaging of Single Molecules of α2-Macroglobulin and the α2-Macroglobulin/Trypsin Complex
- 1 January 1982
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 363 (2) , 803-812
- https://doi.org/10.1515/bchm2.1982.363.2.803
Abstract
From electron micrographs single molecules of human .alpha.2-macroglobulin (.alpha.2M) in the closed form, the open form and as the trypsin complex were computer averaged. The molecular images are discussed. Molecules of the electrophoretically fast migrating F-form have the closed form. In the case of the .alpha.2M/trypsin complex the 2 attached trypsin molecules are located very near to each other and in the central part of the .alpha.2M molecule.This publication has 14 references indexed in Scilit:
- Reactive site in human alpha 2-macroglobulin: circumstantial evidence for a thiolester.Proceedings of the National Academy of Sciences, 1981
- Small-angle X-ray scattering study of human α2-macroglobulinInternational Journal of Biological Macromolecules, 1980
- Structural details of membrane-bound acetylcholine receptor from Tropedo marmorata.Proceedings of the National Academy of Sciences, 1980
- Heat-induced fragmentation of human alpha 2-macroglobulin.Journal of Biological Chemistry, 1979
- Image Analysis In Electron MicroscopyJournal of Microscopy, 1979
- The electrophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin moleculeBiochemical Journal, 1979
- Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coliBiochemistry, 1968
- Electron microscopic studies of some proteins from normal human serumJournal of Molecular Biology, 1965