Methanethiolation of the Liberated Cysteine Residues of Human alpha2-Macroglobulin Treated with Methylamine Generates a Derivative with Similar Functional Characteristics as Native alpha2-Macroglobulin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.tb20180.x/fullpdf
Reference22 articles.
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2. Identification of α2-Macroglobulin as a Cytokine Binding Plasma Protein
3. In support of the trap hypothesis. Chymotrypsin is not rigidly held in its complex with human .alpha.2-macroglobulin
4. Inhibition and partial reversal of the methylamine-induced conversion of "slow" to "fast" electrophoretic forms of human .alpha.2-macroglobulin by modification of the thiols
5. The Combining Ratio between Trypsin and Serum alpha2-Macroglobulin.
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3. Binding of Soluble Myelin Basic Protein to Various Conformational Forms of α2-Macroglobulin;Archives of Biochemistry and Biophysics;1998-11
4. Nonproteolytic Incorporation of Protein Ligands into Human α2-Macroglobulin: Implications for the Binding Mechanism of α2-Macroglobulin;Biochemistry;1998-04-01
5. The Contact Zones in Human alpha2-Macroglobulin. Functional Domains Important for the Regulation of the Trapping Mechanism;European Journal of Biochemistry;1997-03-15
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