V S Pokrovskiĭ, M V Pokrovskaia, S S Aleksandrova, R M Andrianov, D D Zhdanov, N M Omel'ianiuk, E M Treshchalina, N N Sokolov
Index: Prikl. Biokhim. Mikrobiol. 49(1) , 24-8, (2013)
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The physicochemical, catalytic, and antiproliferative activity of a recombinant L-asparaginase from Yersinia pseudotuberculosis (YpA) have been studied. The following results were obtained: the K(M) value for L-asparagine is 17 +/- 0.9 microM, the optimal temperature is 60 degrees C, pH is 8.0, pI is 5.4 +/- 0.3, the L-glutaminase activity is no more than 5-6% of the L-asparaginase activity, and the antiproliferative activity on the Fisher L5178y lymphadenosis cell line comprised T/C = 136% (p < 0.001) at a 15% recovery rate. The described characteristic allows one to regard YpA as an antitumor enzyme with biological features similar to the L-asparaginase of E. coli.
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