Meyer C, Schmid R, Schmieding K, Falkenstein E, Wehling M
Division of Clinical Pharmacology, Klinikum Innenstadt, University of Munich, Germany.
Steroids. 1998 Feb;63(2):111-6. doi: 10.1016/s0039-128x(97)00143-8.
A chemically synthesized 15-mer oligopeptide derived from the N terminus of high affinity progesterone-binding membrane site(s) from porcine liver was used to generate site-specific antibodies. Western blotting experiments confirmed the specificity of the anti-peptide serum obtained. In further investigations this antiserum was used for the identification of the native progesterone-binding membrane protein complex that represents an oligomer with an apparent molecular mass of about 200 kDa. In temperature-induced Triton X-114 phase separation experiments combined with Western-blotting, the progesterone-binding site was identified as an hydrophobic (integral) membrane protein. In addition, in Western blotting analyses the antiserum reacted with the progesterone-binding or related proteins in membrane fractions from a wide array of different tissues in various species.
一种化学合成的15聚体寡肽，其来源于猪肝高亲和力孕酮结合膜位点的N端，用于生成位点特异性抗体。蛋白质印迹实验证实了所获得的抗肽血清的特异性。在进一步的研究中，该抗血清用于鉴定天然孕酮结合膜蛋白复合物，该复合物是一种表观分子量约为200 kDa的寡聚体。在温度诱导的Triton X-114相分离实验与蛋白质印迹相结合的实验中，孕酮结合位点被鉴定为一种疏水（整合）膜蛋白。此外，在蛋白质印迹分析中，该抗血清与来自各种物种的多种不同组织的膜组分中的孕酮结合蛋白或相关蛋白发生反应。
