Functional α2-macroglobulin half-molecules induced by cadmium
- 2 December 1987
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 149 (2), 488-492
- https://doi.org/10.1016/0006-291x(87)90394-9
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Some consequences of the covalent and non-covalent binding modes of plasmin with α2-macroglobulinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Evidence for active half-molecules of .alpha.2-macroglobulin formed by dissociation in ureaBiochemistry, 1987
- Covalent and non‐covalent interaction of chymotrypsin with α2‐macroglobulinFEBS Letters, 1987
- Thrombin-induced conformational changes of human .alpha.2-macroglobulin: evidence for two functional domainsBiochemistry, 1985
- Cadmium binding to human α2-macroglobulinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- The effect of zinc and other divalent cations on the structure and function of human α2-macroglobulinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- HUMAN PLASMA PROTEINASE INHIBITORSAnnual Review of Biochemistry, 1983
- Characterization of functional human .alpha.2-macroglobulin half-molecules isolated by limited reduction with dithiothreitolBiochemistry, 1983
- Human α2-macroglobulin: structure and functionTrends in Biochemical Sciences, 1982
- Purification of human plasma α2 macroglobulin and α1 proteinase inhibitor using zinc chelate chromatographyAnalytical Biochemistry, 1979