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1 t all commercial proteins are purified using ammonium sulfate precipitation.
2 s purified by multistep chromatography after ammonium sulfate precipitation.
3 of 60kDa, was purified to homogeneity using ammonium sulfate precipitation and a series of chromatog
4 from Persian Gulf to homogeneity level using ammonium sulfate precipitation and anion-exchange chroma
5 protein AtzA was purified to homogeneity by ammonium sulfate precipitation and anion-exchange chroma
6 lly defined medium (CDM) and fractionated by ammonium sulfate precipitation and by ion-exchange and g
7 bryonic kidney 293 cell line and purified by ammonium sulfate precipitation and cation exchange chrom
8 protein 23-fold from periplasmic extracts by ammonium sulfate precipitation and chromatographic metho
9 B were purified from culture supernatants by ammonium sulfate precipitation and chromatography throug
10 purified to homogeneity by a combination of ammonium sulfate precipitation and fast protein liquid c
11 tially purified from the supernatant through ammonium sulfate precipitation and gel chromatography, a
12 racted from cornea with urea and purified by ammonium sulfate precipitation and gel chromatography.
13 ment of extracts with Polymin P, followed by ammonium sulfate precipitation and heparin and ion-excha
14 parent homogeneity from culture filtrates by ammonium sulfate precipitation and ion-exchange and mole
15 eins was purified to apparent homogeneity by ammonium sulfate precipitation and liquid chromatography
16 Soybean agglutinin (SBA) was purified using ammonium sulfate precipitation and liquid chromatography
18 from the supernatant of vir-induced cells by ammonium sulfate precipitation and Q-Sepharose chromatog
21 ied from culture supernatants by extraction, ammonium sulfate precipitation, and fast-protein liquid
22 heat treatment (15 min at 90 degrees C), 80% ammonium sulfate precipitation, and gel filtration (Seph
23 ion of DEAE-cellulose column chromatography, ammonium sulfate precipitation, and preparative SDS/PAGE
24 atant to 98% homogeneity by a combination of ammonium sulfate precipitation, anion exchange chromatog
25 ME1 and ME2, were purified to homogeneity by ammonium sulfate precipitation, cation-exchange perfusio
26 -sensitive shedding activity was purified by ammonium sulfate precipitation, DEAE chromatography, and
27 the culture supernatant of this organism by ammonium sulfate precipitation followed by affinity chro
29 uble protein by a simple two-step procedure, ammonium sulfate precipitation followed by DEAE ion-exch
30 ive, allowing a simple purification process (ammonium sulfate precipitation followed by desalting siz
31 -binding proteins were partially purified by ammonium sulfate precipitation followed by heparin agaro
32 ied to homogeneity by ethanol precipitation, ammonium sulfate precipitation, gel-permeation chromatog
33 ielding procedure consisting of three steps: ammonium sulfate precipitation, hydrophobic interaction
34 neutral soluble enamel extract by successive ammonium sulfate precipitations, hydroxyapatite HPLC, re
35 iscera of carp Cirrhinus mrigala (mrigal) by ammonium sulfate precipitation, ion exchange and affinit
36 ferret liver utilizing the following steps: ammonium sulfate precipitation, ion exchange, gel filtra
37 by bioactivity-guided fractionation based on ammonium sulfate precipitation, ion-exchange absorption
40 fied from the WERI-1 cell nuclear extract by ammonium sulfate precipitation, Mono Q chromatography, a
41 ated F1 was partially purified by sequential ammonium sulfate precipitations of a sodium chloride ext
44 ation was achieved by using a combination of ammonium sulfate precipitation, Zn2+ affinity chromatogr