Neil J C, Onions D E, Jarrett O
J Gen Virol. 1980 Oct;50(2):455-60. doi: 10.1099/0022-1317-50-2-455.
Antiserum to the p15(E) polypeptide of Rauscher murine leukaemia virus (R-MuLV) precipitated two proteins from purified virions of feline leukaemia virus (FeLV) with apparent mol. wt. of 18500 and 155000 on SDS-polyacrylamide gels. These proteins have been designated p15(E) and p12(E), in line with the nomenclature for MuLV proteins. Like the analogous protein of MuLV, FeLV p15(E) was found to be disulphide-linked to the virion glycoprotein, gp70. FeLV p15(E) was sensitive to digestion of intact virus particles with the proteolytic enzyme, bromelain, indicating that this protein is on the outer surface of the virion. An analysis of cat sera for precipitating activity for FeLV p12(E) showed this only in sera from cats which had recovered from FeLV infection and had virus-neutralizing activity.
劳氏鼠白血病病毒(R-MuLV)p15(E)多肽的抗血清,在十二烷基硫酸钠-聚丙烯酰胺凝胶上,从纯化的猫白血病病毒(FeLV)病毒粒子中沉淀出两种表观分子量分别为18500和155000的蛋白质。按照鼠白血病病毒蛋白质的命名法,这些蛋白质被命名为p15(E)和p12(E)。与鼠白血病病毒的类似蛋白质一样,发现FeLV p15(E)通过二硫键与病毒粒子糖蛋白gp70相连。FeLV p15(E)对用菠萝蛋白酶消化完整病毒颗粒敏感,这表明该蛋白质位于病毒粒子的外表面。对猫血清进行的针对FeLV p12(E)沉淀活性的分析表明,只有从FeLV感染中恢复且具有病毒中和活性的猫的血清中才有此活性。