Shaginian K A, Shaginian L A, Ianonis V V, Strongin A Ia, Stepanov B M
Biokhimiia. 1981 Jul;46(7):1290-7.
Antibodies against intracellular serine protease and extracellular subtilisin BPN' were raised in rabbits. Using these antibodies and antisera against subtilisin Carlsberg and thermitase (serine protease from Thermoactinomyces vulgaris), it was shown that the proteases of the subtilisin family possess a pronounced immunological variability. Immunological studies demonstrated that the vegetative and sporulating B. amyloliquefaciens cells contain no long-lived protein precursor of intracellular serine protease and that the drastic increase of the enzyme activity during the first hours of the sporulating period is presumably due to its de novo synthesis. The specific protein inhibitor of intracellular serine protease partially purified from B. amyloliquefaciens sporulating cells did not prevent the enzyme interaction with its specific antibodies.
针对细胞内丝氨酸蛋白酶和细胞外枯草杆菌蛋白酶BPN'的抗体在兔子体内产生。使用这些抗体以及针对枯草杆菌蛋白酶卡尔伯格和嗜热栖热放线菌的嗜热酶（丝氨酸蛋白酶）的抗血清，结果表明枯草杆菌蛋白酶家族的蛋白酶具有显著的免疫变异性。免疫学研究表明，解淀粉芽孢杆菌的营养细胞和芽孢形成细胞不含细胞内丝氨酸蛋白酶的长寿蛋白质前体，并且在芽孢形成期的最初几个小时内酶活性的急剧增加可能是由于其从头合成。从解淀粉芽孢杆菌芽孢形成细胞中部分纯化的细胞内丝氨酸蛋白酶的特异性蛋白质抑制剂并不能阻止该酶与其特异性抗体的相互作用。
