Hydrophobic chromatography of proteins using a nitrocellulose membrane.
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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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Membrane-exposed residues are more hydrophobic than buried interior residues in the transmembrane regions of the photosynthetic reaction center from Rhodobacter sphaeroides. This hydrophobic organization is opposite to that of water-soluble proteins. The relative polarities of interior and surface residues of membrane and water soluble proteins are not simply reversed, however. The hydrophobici...
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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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Beta-sheets, in the form of the beta-barrel folding motif, are found in several constitutive membrane proteins (porins) and in several microbial toxins that assemble on membranes to form oligomeric transmembrane channels. We report here a first step towards understanding the principles of beta-sheet formation in membranes. In particular, we describe the properties of a simple hydrophobic hexape...
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ژورنال
عنوان ژورنال: SEIBUTSU BUTSURI KAGAKU
سال: 1989
ISSN: 0031-9082,1349-9785
DOI: 10.2198/sbk.33.305