Ochanda J O, Mumcuoglu K Y, Ben-Yakir D, Okuru J K, Oduol V O, Galun R
Department of Biochemistry, University of Nairobi, Kenya.
Med Vet Entomol. 1996 Jan;10(1):35-8. doi: 10.1111/j.1365-2915.1996.tb00079.x.
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.
人体虱，即人虱（Pediculus humanus），经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分析，显示出18种分子量在12至117 kDa之间的中肠蛋白。其中七种（12 kDa、17 kDa、29 kDa、35 kDa、40 kDa、55 kDa和97 kDa）根据染色强度为主要条带。用中肠提取物免疫兔子可引发保护性多克隆抗体的产生。当通过蛋白质印迹技术检测时，这些抗体与所有主要中肠蛋白以及63 kDa和117 kDa蛋白发生强烈反应。蛋白质分析表明，12 kDa、25 kDa、29 kDa、35 kDa、45 kDa、87 kDa和97 kDa蛋白是糖基化的，且它们均不含脂质部分。通过电洗脱法纯化了35 kDa和63 kDa的蛋白。经胰蛋白酶消化后，35 kDa和63 kDa的蛋白在18% SDS-PAGE上分离时产生了四个主要片段（F1、F2、F3和F4）。35 kDa蛋白的F1片段通过免疫印迹技术与多克隆抗体发生反应。
