Title : Subunits of human alpha 2-macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin.

Pub. Date : 1988 Feb 9

PMID : 2452651






7 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Subunits of human alpha 2-macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin. Disulfides alpha-2-macroglobulin Homo sapiens
2 Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli. Disulfides alpha-2-macroglobulin Homo sapiens
3 Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli. Disulfides alpha-2-macroglobulin Homo sapiens
4 Under the conditions selected, 3.5-4.1 disulfide bonds were cleaved in each alpha 2M molecule, as determined by the consumption of NADPH during the reaction and by the incorporation of iodo[3H]acetate into the reaction product. Disulfides alpha-2-macroglobulin Homo sapiens
5 This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions. Disulfides alpha-2-macroglobulin Homo sapiens
6 This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions. Disulfides alpha-2-macroglobulin Homo sapiens
7 This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions. Disulfides alpha-2-macroglobulin Homo sapiens