Abstract：
:alpha2-Macroglobulin (alpha2M) is a 718 kDa homotetrameric proteinase inhibitor which undergoes a large conformational change upon activation. This conformational change can occur either by proteolytic attack on an approximately 40 amino acid stretch, the bait region, which results in the rupture of the four thioester bonds in alpha2M, or by direct nucleophilic attack on these thioesters by primary amines. Amine activation circumvents both bait region cleavage and protein incorporation, which occurs by proteolytic activation. These different activation methods allow for examination of the roles bait region cleavage and thioester rupture play in alpha2M stability. Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of alpha2M complexes.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Kaczowka SJ,Madding LS,Epting KL,Kelly RM,Cianciolo GJ,Pizzo SVdoi
10.1016/j.ijbiomac.2007.09.019subject
Has Abstractpub_date
2008-01-01 00:00:00pages
62-7issue
1eissn
0141-8130issn
1879-0003pii
S0141-8130(07)00231-0journal_volume
42pub_type
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