Purification of vasoactive intestinal peptide receptor from porcine liver by a newly designed one-step affinity chromatography.
作者： A Couvineau , T Voisin , L Guijarro , M Laburthe
DOI: 10.1016/S0021-9258(19)38310-3
关键词:
摘要: Vasoactive intestinal peptide (VIP) receptors were solubilized from porcine liver membrane using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid. The VIP receptor has been purified approximately 50,000-fold to apparent homogeneity by a one-step affinity chromatography newly designed VIP-polyacrylamide resin. bound 125I-VIP with Kd of 22.3 +/- 0.7 nM and retained its specificity toward VIP-related peptides. specific activity (16,400 pmol/mg protein) was very close theoretical value (18,900 calculated assuming one binding site/protein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed single band an Mr 53,000 after either silver staining or radioiodination. Affinity labeling dithiobis(succinimidyl propionate) gave radioactive band, which completely inhibited excess unlabeled VIP. In conclusion, protein containing VIP-binding site immobilized
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