[Isolation and some properties of transketolase from rat liver].
A new procedure transketolase isolation from rat liver using sievorptive chromatography and adsoption chromatography on hydroxylapatite is described. An enzyme preparation is obtained, which is homogenous under polyacrylamide gel electrophoresis. Molecular weight of native enzyme, estimated by sedimentation equilibrium method, is 130 000. Electrophoresis in polyacrylamide gel in the presence of sodiumdodecylsulphate has revealed a single protein fraction with molecular weight of 70 000. The extinction coefficient A1%1cm at 280 nm is found to be 13. Thiamine pyrophosphate content in native holoenzyme is 1.8--2 moles per 1 mole of protein.
D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology*; D008722:Methods; D008970:Molecular Weight; D051381:Rats; D013056:Spectrophotometry, Ultraviolet; D013835:Thiamine Pyrophosphate / Q000032:analysis; D014174:Transketolase / Q000302:isolation & purification*
D014174:Transketolase; D013835:Thiamine Pyrophosphate
Vydelenie transketolazy iz pecheni krys i nekotorye ee svoĭstva.