人血浆蛋白组分对血小板[3H] - 丙咪嗪结合的抑制作用。

Inhibition of platelet [3H]-imipramine binding by human plasma protein fractions.

作者信息

Strijewski A, Chudzik J, Tang S W

机构信息

Psychopharmacology Unit, Clarke Institute of Psychiatry, Toronto, Ontario, Canada.

出版信息

Life Sci. 1988;42(16):1543-50. doi: 10.1016/0024-3205(88)90012-4.

DOI:10.1016/0024-3205(88)90012-4

PMID:3352466

Abstract

Inhibition of high-affinity [3H]-imipramine binding to platelet membranes by human plasma fractions and isolated plasma proteins was investigated. Several plasma proteins were found to contribute to the observed apparent inhibition and this contribution was assessed in terms of inhibitor units. Alpha 1 acid glycoprotein, high density and low density lipoprotein, IgG and alpha 1-antitrypsin were identified as effective non-specific inhibitors. Alpha-1-acid glycoprotein was confirmed to be the most potent plasma protein inhibitor. Cohn fractions were evaluated for the presence of the postulated endocoid of [3H]-imipramine binding site.

摘要

研究了人血浆组分和分离的血浆蛋白对高亲和力[³H] - 丙咪嗪与血小板膜结合的抑制作用。发现几种血浆蛋白对观察到的表观抑制有作用，并根据抑制剂单位评估了这种作用。α1酸性糖蛋白、高密度和低密度脂蛋白、IgG和α1 - 抗胰蛋白酶被确定为有效的非特异性抑制剂。α1 - 酸性糖蛋白被证实是最有效的血浆蛋白抑制剂。评估了科恩组分中假定的[³H] - 丙咪嗪结合位点内源性物质的存在情况。