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Purification and characterization of uracil phosphoribosyltransferase from Crithidia luciliae.

作者信息

Asai T, Lee C S, Chandler A, O'Sullivan W J

机构信息

School of Biochemistry, University of N.S.W., Kensington, Australia.

出版信息

Comp Biochem Physiol B. 1990;95(1):159-63. doi: 10.1016/0305-0491(90)90264-t.

Abstract
  1. Uracil phosphoribosyltransferase (UPRTase) was purified 370-fold from the protozoan parasite, Crithidia luciliae. 2. The enzyme was a dimer of mol. wt 80 000 and was highly specific for uracil. 3. GTP, which is an activator of UPRTase from E. coli had a slight inhibitory effect on the parasite enzyme. 4. The C. luciliae UPRTase demonstrated a broad specificity for activating divalent metal ions.
摘要

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