Association-dissociation of transcarboxylase.

Transcarboxylase consists of a central subunit to which two sets of three subunits each are attached at opposite faces. Evidence obtained by various ultracentrifugal techniques has shown that there is an equilibrium between active forms of the enzyme with six, five, four, three, two, and one subunits attached to the central subunit. Since each attached subunit contains two biotins, the biotin content of these forms varies from 12 to 2.

A new large form of transcarboxylase with six outer subunits and twelve biotinyl carboxyl carrier subunits.

A new form of transcarboxylase has been isolated which has a molecular weight of 1,200,000, an s20,w of 26 S, and contains 12 biotinyl groups. Transcarboxylase as isolated previously has a molecular weight of 790,000, an s20,w of 18 S, and contains six biotinyl groups. The larger species of enzyme consists of a central hexameric subunit with six dimeric outer subunits attached to it by biotinyl carboxyl carrier proteins, three each at the opposite faces of the central subunits.