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Electron microscopy ofα2-macroglobulin with a thiol ester bound ligand

Authors
Journal
Journal of Structural Biology
1047-8477
Publisher
Elsevier
Publication Date
Volume
108
Issue
3
Identifiers
DOI: 10.1016/1047-8477(92)90022-3
Disciplines
  • Biology

Abstract

Abstract In order to covalently bind the hydrolyzed thiol ester groups of the human α 2-macroglobulin (α2M) transformed by methylamine, the phospholipase A2 (PLA2), a small enzyme ( M r = 13 000) from Naja nigricollis snake venom was activated by succinimidyl 4-(maleimidomethyl)cyclohexane-1-carboxylate (SMCC). Average images determined from electron micrographs of the methylamine-transformed α2M, with and without activated PLA2, were determined by image processing and compared. A localization of the PLA2 was achieved by subtracting the average image of α2M transformed by methylamine from that containing PLA2. The results are consistent with previous work showing the central localization of chymotrypsin trapped in α2M. They also suggest that the four thiol esters are located near the center of the α2M. molecule.

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