β Scribed by K.-H. Pawlizki; G.J. Kelly; E. Latzko
No coin nor oath required. For personal study only.
Low levels of sulfonated polystyrene, a possible contaminant of cationexchange resins, inhibited several dehydrogenase enzymes including glyceraldehyde-3-phosphate dehydrogenase from chloroplasts (but not that from rabbit muscle) and glucose-6-phosphate dehydrogenase from yeast. Less than 3 ppm sulfonated polystyrene reduced the activities of these enzymes by 50%. Relatively high concentrations of monovalent cations relieved the inhibitions.
π SIMILAR VOLUMES
The heterogeneous acetal-based membranes containing 50, 60, 70, 80, and 90% (w/w) of the sulfonated polystyrene crosslinked with 7% divinyl benzene were fabricated and studied. In addition, the heterogeneous acetal-based membranes of 85% (w/w) sulfonated polystyrene crosslinked with 1, 4, and 7% div
An ion exchange method for the separation of pure 22Na from bombarded Mg targets has been developed. Mg is complexed by citrate at a pH of 8 in a 40% methanol solution and is eluted, while 22Na is retained on the resin. Triethanolamine is used for pH adjustment. 22Na is eluted with ammonium carbonat