Subunit interactions of transcarboxylase as studied by circular dichroism
- 16 February 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (4) , 642-646
- https://doi.org/10.1021/bi00533a007
Abstract
A change in the secondary structure of transcarboxylase [from propionic acid bacteria] resulting from quaternary interactions is monitored by circular dichroism [CD] spectroscopy. The change is traced to interactions among the 6 polypeptides that make up the 12SH subunit. It is fully reversible and is not a result of the conditions used to dissociate the enzyme. A new method of analyzing CD spectra for secondary structure works well for this enzyme and its subunits. Even the odd CD of the 1.3SE subunit analyzes well. There is an increase of 19% in .alpha.-helix and a concomitant decrease of 8% in antiparallel .beta.-sheet and 7% in random structure on association to form the hexameric 12SH subunit.This publication has 1 reference indexed in Scilit:
- A new large form of transcarboxylase with six outer subunits and twelve biotinyl carboxyl carrier subunits.Journal of Biological Chemistry, 1977