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

@article{Mandrell1993DetectionAS,
  title={Detection and some properties of the sialyltransferase implicated in the sialylation of lipopolysaccharide of Neisseria gonorrhoeae.},
  author={Robert E. Mandrell and Harry Smith and Gary A Jarvis and John Mcleod Griffiss and Jeff A. Cole},
  journal={Microbial pathogenesis},
  year={1993},
  volume={14 4},
  pages={307-13}
}
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… CONTINUE READING

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