Zsürger N, Mazella J, Vincent J P
Institut de Pharmacologie Moléculaire et Cellulaire du CNRS, Valbonne, France.
Brain Res. 1994 Mar 14;639(2):245-52. doi: 10.1016/0006-8993(94)91737-x.
High affinity neurotensin receptors were solubilized in an active form from newborn human brain using the non-denaturing detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). The solubilized receptor was purified in a single step by affinity chromatography. The binding properties of the purified receptor towards [125I-Tyr3]neurotensin are very similar to those of the membrane bound and of the crude CHAPS-solubilized receptor in terms of affinity and specificity. The purified receptor is a single protein chain of molecular weight 100 kDa as shown by gel filtration and by affinity labelling with [125I-Tyr3]neurotensin in the presence of the cross-linking agent disuccinimidyl suberate.
使用非变性去污剂3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸（CHAPS），从新生人类大脑中以活性形式溶解高亲和力神经降压素受体。通过亲和色谱法一步纯化溶解的受体。纯化后的受体对[125I-Tyr3]神经降压素的结合特性在亲和力和特异性方面与膜结合受体以及粗制CHAPS溶解受体的结合特性非常相似。凝胶过滤以及在交联剂辛二酸二琥珀酰亚胺酯存在下用[125I-Tyr3]神经降压素进行亲和标记显示，纯化后的受体是一条分子量为100 kDa的单蛋白链。
