Hydrophobic chromatography of proteins on polyvinylalcohol beads column.
نویسندگان
چکیده
منابع مشابه
Hydrophobic Affinity Chromatography of Proteins
1. Chromatographic studies have been made of the affinities of a number of purified proteins for agarose (Sepharose 4B) substituted with 4-phenylbutylamine (PBA) or with E-aminocaproyl-n-tryptophan methyl ester (ACTME) as compared to controls of untreated agarose and/or of cyanogen bromide treated agarose without addition of a substituting amine. 2. At pH 8, cu-chymotrypsin (3.4.4.5) and 7s y-g...
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A method is described for the chromatographic separation of mixtures of egg-yolk proteins of low solubility, by using a hydrophobic column (phenyl-Sepharose) and eluting with increasing concentrations of aqueous urea at low pH. The resolving power of the method was established by tests on proteins and protein fragments of known sequence. The theoretical basis for the method remains, however, un...
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5' tritylated oligonucleotides binding hydrophobically to low trityl cellulose/sepharose (< 15 microMTr/ml) retain their hydrogen-bonding specificities for complementary sequences. This, constitutes a novel mode of attaching affinity ligands to solid supports, is more convenient than existing methods, and proceeds with 100% yield. The salt, dielectric constant and temperature dependence of thes...
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Nuclear proteins modified by mono or poly ADP-ribosylation were selectively isolated and purified by covalent chromatography on a dihydroxyboryl polyacrylamide bead column that specifically interacts with cis-diol-containing compounds. From rat liver nuclei that had been incubated with NAD+, histones and some nonhistone proteins were extracted with 0.25 M HCl. Approximately 60% of the ADP-ribos...
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ژورنال
عنوان ژورنال: BUNSEKI KAGAKU
سال: 1988
ISSN: 0525-1931
DOI: 10.2116/bunsekikagaku.37.12_659