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1 xtracts from 293S cells were fractionated on phosphocellulose.
3 displays the same purification profile over phosphocellulose and DNA affinity resins and has the sam
6 ith purified Rep78, RPA, RFC, and PCNA and a phosphocellulose chromatography fraction (IIA) that cont
7 ated as single peaks from DEAE-Sepharose and phosphocellulose chromatography gave separate peaks of m
9 When the expressed L protein was purified by phosphocellulose column chromatography, it eluted in two
13 -step fractionation of crude extracts on P11 phosphocellulose, followed by (ii) a discrete series of
15 biochemically complemented by a crude TFIID phosphocellulose fraction, indicating that hnRNP K might
17 t cells by chromatography on DEAE-cellulose, phosphocellulose, heparin-agarose, and single-stranded D
18 activates the right-hand hairpin elutes from phosphocellulose in high salt, has a molecular mass of a
20 s separation of phosphorylated peptides with phosphocellulose membranes, and extensive washing steps.
21 separated from endogenous DNA polymerases by phosphocellulose, Mono Q-Sepharose, and single-stranded
22 2 peptides was not observed using either the phosphocellulose paper absorption method or electrospray
23 gen copurified and coimmunoprecipitated with phosphocellulose-purified TFIID from SV40-infected alpha
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