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Enzymology: equilibrium constant

Selected entries from Methods in Enzymology [vol, page(s)] Acetate assay with, 3, 269 activation, 44, 889 activity assay, 44, 893, 894 alternative substrates, 87, 11 bridge-to-nonbridge transfer, 87, 19-20, 226, 232 chiral phosphoryl-ATP, 87, 211, 258, 300 cold denaturation, 63, 9 cysteine residues, 44, 887-889 equilibrium constant, 63, 5 exchange properties, 64, 9, 39, 87,... [Pg.7]

Selected entries from Methods in Enzymology [vol, page(s)] Buffer capacity, 63, 4 choice, 63, 19, 20, 285 metal ion chelation effects, 63, 225, 226, 287, 298, 299 dielectric constant effect on pK, 63, 226 dilution, 63, 20 equilibrium constant effects, 63, 18 heavy water, 63, 226, 227 ionic strength effects, 63, 226,... [Pg.102]

A-Acetyl neuraminic acid aldolase [from Clostridium perfringens, A-acetylneuraminic acid pyruvate lyase] [9027-60-5] [EC 4.1.3.3]. Purified by extraction with H20, protamine pptn, (NH4)2S04 pptn, Me2CO pptn, acid treatment at pH 5.7 and pptn at pH 4.5. The equilibrium constant for pyruvate + n-acetyl-D-mannosamine ++ /V-acetylneuraminidate at 37° is 0.64. The Km for A-acetylneuraminic acid is 3.9mM in phosphate at pH 7.2 and 37°. [Comb and Roseman Methods in Enzymology 5 391 1962). The enzyme from Hogg kidney (cortex) has been purified 1700 fold by extraction with H20, protamine sulphate pptn, (NH4)2S04 pptn, heat treatment between 60-80°, a second (NH4)2S04 pptn and starch gel electrophoresis. The Km for A-acetylneuraminic acid is 1.5mM. [Brunetti et al. JBC 237 2447 1962). [Pg.460]


See other pages where Enzymology: equilibrium constant is mentioned: [Pg.44]    [Pg.460]    [Pg.259]    [Pg.2]    [Pg.176]    [Pg.182]    [Pg.59]    [Pg.32]    [Pg.168]    [Pg.520]    [Pg.304]    [Pg.687]    [Pg.285]    [Pg.72]   
See also in sourсe #XX -- [ Pg.408 ]




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