Title : The electrophoretically 'slow' and 'fast' forms of the alpha 2-macroglobulin molecule.

Pub. Date : 1979 Aug 1

PMID : 91367






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Electrophoresis of S-alpha 2M in the presence of sodium dodecylsulphate gave results consistent with the view that the alpha 2M molecule is a tetramer of identical subunits, assembled as a non-covalent pair of disulphide-linked dimers. disulphide alpha-2-macroglobulin Homo sapiens
2 Exposure of S-alpha 2M to 3 M-urea or pH3 resulted in dissociation to the disulphide-bonded half-molecules; these did not show the proteinase-binding activity characteristic of the intact alpha 2M. disulphide alpha-2-macroglobulin Homo sapiens
3 F-alpha 2M formed by reaction with a proteinase or ammonium salts was not dissociated under the same conditions, although the interchain disulphide bonds were reduced. disulphide alpha-2-macroglobulin Homo sapiens