Reconstitution of bovine procarboxypeptidase A-S6 from the free subunits.

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

Biochemistry

journal_title

Biochemistry

authors

Puigserver A,Desnuelle P

doi

10.1021/bi00630a028

subject

Has Abstract

pub_date

1977-05-31 00:00:00

pages

2497-501

issue

11

eissn

0006-2960

issn

1520-4995

journal_volume

16

pub_type

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