Podboronov V M
Med Parazitol (Mosk). 1990 May-Jun(3):21-3.
Using a technique based on specific enzyme sorption by chitin (beta-1-4-N-acetylglucosamine), lysozyme with a molecular mass of 15,000 has been isolated from homogenates of the Ix. persulcatus ticks. Micrococci and staphylococci proved to be most sensitive to lysozyme from the Ix. persulcatus ticks, while E. coli and Salmonella were less sensitive. The minimum inhibitory concentration of lysozyme from Ix. persulcatus was 2-4 times lower than that of egg lysozyme. Lysozyme from the Ix. persulcatus ticks is resistant to heating in acid medium and loses some of its activity in alkaline medium. The loss of the activity in the both media is somewhat lower than that of egg lysozyme in analogous conditions.
利用基于几丁质(β-1-4-N-乙酰葡糖胺)对特定酶的吸附技术,从全沟硬蜱匀浆中分离出了分子量为15,000的溶菌酶。事实证明,微球菌和葡萄球菌对全沟硬蜱的溶菌酶最为敏感,而大肠杆菌和沙门氏菌则不太敏感。全沟硬蜱溶菌酶的最低抑菌浓度比鸡蛋溶菌酶低2至4倍。全沟硬蜱的溶菌酶在酸性介质中耐热,在碱性介质中会丧失部分活性。在这两种介质中的活性丧失程度均略低于类似条件下鸡蛋溶菌酶的活性丧失程度。