Abstract:
:The three subunits I, II, and III of bovine procarboxypeptidase A separated by reversible dimethylmaleylation can reassociate to form the reconstituted complexes I + II, I + III, and I + II + III. Since the association II + III is not possible, subunit I appears to play a central role in the formation of the complex. It is suggested that subunit I possesses two independent and specific sites for the recognition of subunits II and III. The liberation of subunit I from any of the complexes was observed to increase its activability, although to a lesser extent than predicted by assays carried out with the succinylated protein. By contrast, the bound form of subunit II was activated faster than the free form. The potential activity of the bound form and the activity of the preformed endopentidase were also higher, suggesting a conformational change induced by association. This suggestion was fully supported by the observed modifications of the heat stability and intrinsic fluorescence spectrum of the subunit resulting form association.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Puigserver A,Desnuelle Pdoi
10.1021/bi00630a028subject
Has Abstractpub_date
1977-05-31 00:00:00pages
2497-501issue
11eissn
0006-2960issn
1520-4995journal_volume
16pub_type
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