Valine-sensitivity as well as activity of acetolactate synthase of Neurospora crassa was stabilized with 1.2 M potassium phosphate buffer during extraction from mitochondria and early stages of purification, and with 20% glycerol plus 5 mM sodium pyruvate during Sephadex G200 gel chromatography. The enzyme was expressed as four molecular species having the molecular weights of about 500,000, 140,000, 68,000 and 51,000, respectively. The first and the third species showed valine-sensitivity, but the second and the fourth did not. The third molecular species with a molecular weight of 68,000 may be the basal unit of valine-sensitive acetolactate synthase of Neurospora crassa.

Download full-text PDF

Source
http://dx.doi.org/10.1016/0006-291x(84)90246-8DOI Listing

Publication Analysis

Top Keywords

acetolactate synthase
12
synthase neurospora
12
neurospora crassa
12
basal unit
8
unit valine-sensitive
8
valine-sensitive acetolactate
8
molecular species
8
species molecular
8
crassa valine-sensitivity
4
valine-sensitivity well
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!