Detection and some properties of the sialyltransferase implicated in the sialylation of lipopolysaccharide of Neisseria gonorrhoeae.
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.
Mandrell
R E
RE
Centre for Immunochemistry, Veterans Administration Medical Center/113A, San Francisco, CA 94121.
Smith
H
H
Jarvis
G A
GA
Griffiss
J M
JM
Cole
J A
JA
D003470:Culture Media; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000378:metabolism; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008070:Lipopolysaccharides / Q000378:metabolism*; D009344:Neisseria gonorrhoeae / Q000201:enzymology*; D017830:Octoxynol; D011092:Polyethylene Glycols; D012799:Sialyltransferases / Q000378:metabolism*; D013696:Temperature
D003470:Culture Media; D008070:Lipopolysaccharides; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D011092:Polyethylene Glycols; D017830:Octoxynol; D012799:Sialyltransferases