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Microb Pathog. 1993 Apr;14(4):307-13.

Detection and some properties of the sialyltransferase implicated in the sialylation of lipopolysaccharide of Neisseria gonorrhoeae.

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Centre for Immunochemistry, Veterans Administration Medical Center/113A, San Francisco, CA 94121.


A sensitive assay for sialyltransferase (STase activity extracted from gonococci with 0.5% Triton X100 was developed. Enzyme activity was optimal in the pH range 5.8-8.0 and was strongly inhibited by CMP, CDP and CTP, but not by other nucleotides, 10 mM Mg2+, Zn2+, Ca2+ or Mn2+, or by 18 mM EDTA. More than 90% of the activity was lost after 30 s at 67 degrees C. The apparent Vmax and apparent Km of the STase for cytidine 5'-monophospho-N-acetylneuraminic acid were 1.7 nmol of NANA incorporated/min/mg protein and 5.3 microM, respectively.

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