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- W994066688 abstract "This chapter describes the assay method, purification procedure, and properties of triosephosphate isomerase from rabbit liver. The enzyme is assayed spectrophotometrically. The purification procedure includes the preparation of initial extract, ammonium sulfate fractionation, chloroform and ethanol fractionation, DEAE-Sephadex chromatography, CM-sephadex chromatography and crystallization, and QAE-sephadex chromatography and recrystallization. The purified liver enzyme shows in starch and polyacrylamide gel electrophoresis three major forms (95%–98% of total protein) and two minor forms. The five isoenzymes have the same electrophoretic mobility as those of the rabbit muscle triosephosphate. The purified enzyme preparation retains all its activity for at least two years if kept at 4° in 2.5 M ammonium sulfate and 1 mM EDTA at pH 7.0. isomerase. Rabbit liver and muscle triosephosphate isomerase have identical kinetic properties. As for the yeast and the muscle triosephosphate isomerase, the following reagents act as inhibitors also for the liver enzyme: arsenite, phosphate, phosphoenolpyruvate, D-α-glycerophosphate, acetylphosphate, phosphoglycollate, and D-erythrose-4-phosphate. Triosephosphate isomerase of liver and muscle is inhibited by sulfhydryl and alkylating agents and by photo-oxidation." @default.
- W994066688 created "2016-06-24" @default.
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- W994066688 date "1975-01-01" @default.
- W994066688 modified "2023-09-26" @default.
- W994066688 title "[93] Triosephosphate isomerase from rabbit liver" @default.
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- W994066688 doi "https://doi.org/10.1016/s0076-6879(75)41095-3" @default.
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