Heymer B, Schmidt W C
Microbios. 1975;12(47-48):51-66.
The purification and characterization of the streptolytic exo-enzyme from the Maxted-McCarty strain of Streptomyces albus is described. This enzyme was shown to be an endo-N-acetylmuramidase with a molecular weight of 10 to 12,000 and optimal activity at pH 8 and 45 degrees C. The enzyme is lytic for streptococci of various groups, Micrococcus lysodeikticus, Staphylococcus aureus, as well as Escherichia coli. It closely resembles the F1 endo-N-acetylmuramidase described by Ghuysen et al. (1966) except for small differences in the products of lysis of streptococcal cell walls and the resistance of Escherichia coli to lysis by the F1 enzyme. Lysates of group A and A variant streptococcal cell walls prepared with purified Streptomyces albus muramidase contained serologically active M protein and C carbohydrate-peptidoglycan complexes. The chemical and immunological characteristics of these enzymmatic products of streptococcal cell walls are reported and their utility as immunologic reagents is described.
本文描述了从白色链霉菌马克斯泰德-麦卡蒂菌株中纯化和鉴定链溶外切酶的过程。该酶被证明是一种内切N-乙酰胞壁酸酶，分子量为10至12,000，在pH 8和45℃时具有最佳活性。该酶对各种链球菌、溶壁微球菌、金黄色葡萄球菌以及大肠杆菌均有裂解作用。除了在链球菌细胞壁裂解产物以及大肠杆菌对F1酶裂解的抗性方面存在细微差异外，它与Ghuysen等人（1966年）描述的F1内切N-乙酰胞壁酸酶极为相似。用纯化的白色链霉菌胞壁酸酶制备的A组和A变体链球菌细胞壁裂解物含有血清学活性的M蛋白和C碳水化合物-肽聚糖复合物。报告了这些链球菌细胞壁酶解产物的化学和免疫学特性，并描述了它们作为免疫试剂的用途。
