7 research outputs found
Assays for the measurement of tissue transglutaminase (type II) mediated protein crosslinking via ϵ-(γ-glutamyl) lysine and N′,N′-bis (γ-glutamyl) polyamine linkages using biotin labelled casein
Lysine-sensitive plant aspartate kinase is not regulated by calcium or calmodulin
AbstractLysine-sensitive plant aspartate kinase purified from Daucus carota to a specific activity 20-fold higher than previously reported was not activated by calcium or calmodulin. The calmodulin antagonists calmodazolium and compound 4880 did not inhibit activity. However, trifluoperazine exhibited an inhibitory effect, but only at high concentrations. The results do not agree with a previous proposal that calcium and calmodulin play a key role in regulating higher plant lysine-sensitive aspartate kinase
Effects of phenyl saligenin phosphate on cell viability and transglutaminase activity in N2a neuroblastoma and HepG2 hepatoma cell lines
Determination of aspartate kinase in maize tissues.
Lysine, threonine, methionine and isoleucine are synthesized from aspartate in a branched pathway in higher plants. Aspartate kinase plays a key role in the control of the aspartate pathway. The enzyme is very sensitive to manipulation and storage and the hydroxamate assay normally used to determine aspartate kinase activity has to be altered according to the plant species and tissue to be analyzed. We have optimized the assay for the determination of aspartate kinase in maize plants callus cell cultures. Among all the assay parameters tested, the concentration of ATP/Mg and temperature were critical for enzyme activity. In the case of temperature, 35°C was shown to be the optimum temperature for aspartate kinase activity
