Published in Women's Health Weekly, November 13th, 2003
"AMP-deaminase from human term placenta was chromatographed on a phosphocellulose column and physico-chemical and immunological properties of the purified enzyme were investigated," investigators in Poland report.
"At physiological pH 7.0, in the absence of regulatory ligands (control conditions) studied AMP-deaminase manifested sigmoid-shaped substrate saturation kinetics, with half-saturation parameter (S-0.5) value of about 7 mM.
"Addition of important allosteric effectors (ATP, ADP or orthophosphate) modified kinetic properties of studied...
Want to see the full article?
Welcome to NewsRx!
Learn more about a six-week, no-risk free trial of Women's Health Weekly
NewsRx also is available at LexisNexis, Gale, ProQuest, Factiva, Dialog, Thomson Reuters, NewsEdge, and Dow Jones.