Severin A I, Tauson E L, Stepnaia O A, Kulaev I S
Prikl Biokhim Mikrobiol. 1988 Mar-Apr;24(2):187-92.
Specificity of Staphylococcus aureus 209P cell wall hydrolysis by a lytic preparation isolated from the culture liquid filtrate of Pseudomonas lytica VKM V-1454D was studied by the dansylation method. The lytic preparation was found to contain the lytic proteinase lysing the cells of Gram-positive microorganisms. The enzyme hydrolysed the cell walls of S. aureus 209P releasing N-terminal glycine and alanine in amounts of 0.73 and 0.34 mumoles per 1 mumole of lysine, respectively, which indicated the cleavage of the bonds in the pentaglycine bridge and, apparently, of the bond between N-acetylmuramic acid.
采用丹磺酰化法研究了从解磷假单胞菌VKM V - 1454D培养液滤液中分离得到的一种溶菌制剂对金黄色葡萄球菌209P细胞壁的水解特异性。发现该溶菌制剂含有能裂解革兰氏阳性微生物细胞的溶菌蛋白酶。该酶水解金黄色葡萄球菌209P的细胞壁，每1微摩尔赖氨酸分别释放出0.73和0.34微摩尔的N - 末端甘氨酸和丙氨酸，这表明五肽甘氨酸桥中的键以及显然还有N - 乙酰胞壁酸之间的键发生了断裂。
