Autilio-Gambetti L, Crane R, Gambetti P
J Neurochem. 1986 Feb;46(2):366-70. doi: 10.1111/j.1471-4159.1986.tb12977.x.
Cleavage at cysteine and chymotrypsin digestion were applied to two human neurofilament (NF) subunits, low- and high-molecular-weight NF (NF-L and NF-H), to locate the regions reacting with Bodian's silver stain and with several monoclonal antibodies, including NF-specific antibodies and one that recognizes all intermediate filaments (anti-IFA). Our findings indicate that whereas anti-IFA recognizes the highly conserved rod domain, all the NF-specific antibodies, as well as Bodian's silver, react with the carboxy-terminal tailpiece of NF subunits. The silver binding sites in NF-L are located in a carboxy-terminal 12-Kd chymotrypsin fragment, a highly charged, unique domain of NF.
对两种人类神经丝(NF)亚基,即低分子量和高分子量神经丝(NF-L和NF-H)进行半胱氨酸切割和胰凝乳蛋白酶消化,以定位与博迪安银染以及几种单克隆抗体反应的区域,这些单克隆抗体包括NF特异性抗体和一种识别所有中间丝的抗体(抗中间丝抗体,anti-IFA)。我们的研究结果表明,抗中间丝抗体识别高度保守的杆状结构域,而所有NF特异性抗体以及博迪安银染均与NF亚基的羧基末端尾段发生反应。NF-L中的银结合位点位于羧基末端一个12千道尔顿的胰凝乳蛋白酶片段中,该片段是NF一个高度带电的独特结构域。