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-Reference-Cited by-同舟云学术

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

Published:1990-02-13 Issue:6 Volume:29 Page:1638-1643
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cunningham Leon W.,Crews Brenda C.,Gettins Peter

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00458a040

Reference45 articles.

1. The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

2. The electrophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin molecule

3. Binding of proteinases to human α2-macroglobulin with its thioester bonds cleaved by methylamine in the presence of a thiol-group-cyanylating reagent

4. Evidence for similar conformational changes in α2-macroglobulin on reaction with primary amines or proteolytic enzymes

5. Changes of the proteinase binding properties and conformation of bovine .alpha.2-macroglobulin on cleavage of thio ester bonds by methylamine

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