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1 d influences the ability of hsp90 to bind to phenyl-Sepharose.
2 the ATP-bound state lowers its affinity for phenyl-Sepharose.
3 ated from galactokinase by chromatography on phenyl-Sepharose.
4 s p23 and Hop, and to the hydrophobic resin, phenyl-Sepharose.
5 biquinone reductase by a procedure involving phenyl-Sepharose 4B column chromatography, preparative S
7 phobic interaction, Mono Q, hydroxylapatite, phenyl-Sepharose, and chromatofocusing fast protein liqu
9 was purified by chromatography on DE-52 and phenyl-Sepharose, and its steady-state kinetic constants
11 y for p23 and decreased affinity for Hop and phenyl-Sepharose, are brought on by ATP binding alone.
12 ands from trypsin cleavage and increased the phenyl-Sepharose binding of a recombinant DGK alpha frag
15 act with phenyl-Sepharose, indicating that a phenyl-Sepharose-binding region (PSBR) of recS100A1 had
17 sulted in the separation of two fractions by phenyl-Sepharose chromatography, both of which phosphory
18 hydrophobic-interaction chromatography with phenyl-Sepharose CL-4B and gel filtration with Sephacryl
19 purified by ammonium sulfate fractionation, phenyl-Sepharose column chromatography, F420-ether-linke
20 ication was performed using Con-A Sepharose, Phenyl Sepharose, DEAE Sephacel, and Superdex 75 FPLC.
21 eparation included sequential DEAE-Sephacel, phenyl-Sepharose FF, heparin-Sepharose CL-6B, and Q-Seph
22 ng hydrophobic interaction chromatography on phenyl Sepharose followed by anion-exchange chromatograp
23 domonas palustris by sequential Q-Sepharose, phenyl-Sepharose, gel filtration, and hydroxyapatite chr
24 cts of the cells by chromatography on DE-23, phenyl-Sepharose, heparin-agarose, and butyl-Sepharose.
25 tography using SP-Sepharose cation exchange, phenyl-Sepharose hydrophobic interaction, concanavalin A
26 ent extraction, DEAE-Sepharose ion exchange, Phenyl-Sepharose hydrophobic interaction, Sephadex G-100
28 the Delta85-93 protein did not interact with phenyl-Sepharose, indicating that a phenyl-Sepharose-bin
30 studies using Escherichia coli-expressed and phenyl-Sepharose-purified CaM mutants revealed that the
31 monium sulfate fractionation, DEAE-Sephacel, phenyl-Sepharose, S-Sepharose, Sephadex G-75, concanaval
32 wed by column chromatography successively on phenyl-Sepharose, Sephadex G-200, and twice on Mono Q FP
33 aller PP4 complex was purified by sequential phenyl-Sepharose, Source 15Q, DEAE2, and Superdex 200 ge
34 tosol treated with N-ethylmaleimide (NEM) or phenyl-Sepharose to inactivate or deplete Crm1, respecti
35 d reduced calcium-dependent interaction with phenyl-Sepharose when compared with recS100A1, demonstra
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