[Isolation and purification of histone-specific acetyltransferases from the rat liver].
There forms of histone-specific acetyltransferases--A, B and C are obtained from the rat liver nuclei. The isolation process included nuclei generation, ammonium sulphate salting-out of proteins, DEAE-cellulose, hydroxyl-apatite, phosphocellulose chromatography and Sephadex C-200 gel-filtration. Acetyltransferases A, B and C from the nuclei were purified 56.8, 144.1 and 42.3 times, respectively. Histones were preferential substrates of the obtained enzymes. Molecular mass of acetyltransferases was determined by Sephadex G-150 and G-200 gel-filtration. It was 120 for enzyme A, about 90 for B and above 200 kDa for C.
D000123:Acetyltransferases / Q000302:isolation & purification*; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D051548:Histone Acetyltransferases; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins
D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases
Vydelenie i ochistka gistonspetsifichnykh atsetiltransferaz iz pecheni krys.