Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure -- Qiu and Davidson 97 (1): 97 Data Supplement - Supplemental Figure -- Proceedings of the National Academy of Sciences

Supplementary material for Qiu and Davidson (2000) Proc. Natl. Acad. Sci. USA 97 (1), 97-102.

Fig. 6.
Enzymatic activities of fractions from glycerol gradient sedimentation. Wild-type CPSase-ATCase-DHOase polypeptide (CAD) (u) and CAD-R269A (¡) were sedimented on an 8-30% (wt/vol) glycerol gradient with 25 mM MgCl₂. Each fraction was assayed individually for CPSase (A), ATCase (B), and DHOase (C).