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- W2112089969 abstract "Proteolipids (i.e., hydrophobic proteins) have been extracted with chloroform-methanol (2:1) from lyophilized Torpedo electroplax, and fractionated on a DEAE-cellulose column. The elution system consisted of the same solvent and a gradient of the hydrophobic ion ptoluene sulfonate (0.1–100mM). The three fractions obtained (I, II and III) have different content of protein, lipid P, and reducing sugars. The amino acid composition shows a higher proportion of hydrophobic residues in I and more charged ones in fractions II and III. Polyacryl amide gel electrophoresis of fraction I shows a single major band of 39 kdaltons; in fractions II and III a major band of 42 kdaltons and fainter bands in the range 62–68 kdaltons are observed.Fraction I has the highest specific binding for [3H]-acetylcholine (7.1 nmol/mg protein) and [3H]α-bungarotoxin (5.2 nmol/mg protein). The nicotinic nature of this proteolipid was demonstrated by blocking experiments. The Scatchard plot showed two affinity sites for [3H]-acetylcholine (Kd1 = 3nM and Kd2 = 1.1 μm). 4-(N-maleimido) pheny1 [3H]trimethylammonium specifically labeled the 39 kdaltons band.The possible factors involved in the fractionation of proteolipids are discussed. The findings suggest that the 39 kdaltons polypeptide contains the receptor site for acetylcholine and that the other proteolipid components may play a different function in the membrane." @default.
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- W2112089969 date "1980-01-01" @default.
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- W2112089969 title "Cholinergic Binding to the Receptor Proteolipid fromTorpedoElectroplax Separated by Ion Exchange Chromatography" @default.
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- W2112089969 doi "https://doi.org/10.3109/10799898009044097" @default.
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