Tripolyphosphatase associated with S-adenosylmethionine synthetase isozymes from rat liver.
S-Adenosylmethionine (AdoMet) synthetase alpha and beta were purified to homogeneity, as judged by SDS-polyacrylamide gel electrophoresis from rat liver. When the purified enzymes were applied onto Sephacryl S-200, each synthetase was eluted together with a tripolyphosphatase. The activities of these isozymes in synthesizing AdoMet and in hydrolyzing tripolyphosphate decreased in parallel with increasing amounts of rabbit anti-(beta-form) IgG. The activity of the beta-form isozyme was markedly stimulated by the addition of tripolyphosphate, whereas that of the alpha-form isozyme was inhibited. The tripolyphosphatase activity of both the alpha- and the beta-form was markedly stimulated by the addition of AdoMet. The tripolyphosphatases of each isozyme showed some other similar properties.
D017766:Acid Anhydride Hydrolases; D000818:Animals; D002850:Chromatography, Gel; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008716:Methionine Adenosyltransferase / Q000378:metabolism*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D014166:Transferases / Q000378:metabolism*
D007527:Isoenzymes; D009097:Multienzyme Complexes; D014166:Transferases; D008716:Methionine Adenosyltransferase; D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C023193:tripolyphosphatase