Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity-Reference-Cited by-同舟云学术

Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity

Published:1981-06-01 Issue:1 Volume:128 Page:123-126
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sottrup-Jensen Lars,Petersen Torben E.,Magnusson Staffan

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(81)81096-4/fullpdf

Reference30 articles.

1. Characterization of alkylamine-sensitive site in alpha 2-macroglobulin.

2. A thiol-ester in α2 -macroglobulin cleaved during proteinase complex formation

3. Sequence location of the reactive thiol ester in human α2 -macroglobulin

4. Third component of human complement: structural requirements for its function

5. Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement.

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