从蛙脑中纯化κ-阿片受体亚型至表观均一性。
Purification of kappa-opioid receptor subtype to apparent homogeneity from frog brain.
作者信息
Borsodi A, Khan A, Simon J, Benyhe S, Hepp J, Wollemann M, Medzihradszky K
机构信息
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged.
出版信息
NIDA Res Monogr. 1986;75:1-4.
PMID:2828951
Abstract
Kappa-opioid receptor subtype was purified from digitonin solubilized preparation of frog brain membranes by hydrophobic and Sepharose 6B chromatography. 4800-fold purification over the membrane-bound receptors was achieved. The kappa receptor activity resides in a homo-oligomer of a single polypeptide of Mr 65,000.
摘要
κ-阿片受体亚型是通过疏水色谱和琼脂糖凝胶6B色谱从洋地黄皂苷增溶的蛙脑膜制剂中纯化得到的。相对于膜结合受体实现了4800倍的纯化。κ受体活性存在于一条分子量为65,000的单一多肽的同型寡聚体中。
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