| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5167932 | Phytochemistry | 2005 | 7 Pages |
Abstract
Certain buffers and molecular crowding conditions had strong effects on oligomerization status of purified recombinant barley UDP-glucose pyrophosphorylase (UGPase). This in turn could affect the activity of the protein which is active only as monomer. The data are discussed with respect to molecular determinants of structure/function properties of UGPase.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Leszek A. Kleczkowski, Françoise Martz, Malgorzata Wilczynska,