| Popis: |
Aspartate kinase (EC 2.7.2.4) has been extracted and partially purified from actively growing suspension cultures derived from root tissue of Daucus carota L. The specific activity of the preparations was about ten-fold higher than those reported from other higher plant sources. A variable proportion, up to 24%, of the activity was inhibited by 1 mM L-threonine, and the remainder by 5 mM L-lysine. These inhibitions were independent adn additive for combinations of lysine and threonine. The other aspartate-derived amino acids, homoserine, isoleucine and methionine, were without effect. Of a range of structural lysine analogues tested at 10 mM. only S-2-aminoethyl-L-cysteine inhibited the lysine-sensitive activity completely. |
