Abstract
By a combination of protamine sulfate treatment, ammonium sulfate fractionation, gel filtration and hydrophobic interaction chromatography, an active δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase from the prokaryoteStreptomyces clavuligerus was purified 135-fold to give a single major protein band on SDS-PAGE. Its size appears to be approximately 360 kDa which is very similar to that of the enzyme from the eukaryote,Cephalosporium acremonium.
Full Text
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call