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pubmed:abstractText |
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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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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