Sudo S, Dworkin M
J Bacteriol. 1972 Apr;110(1):236-45. doi: 10.1128/jb.110.1.236-245.1972.
The bacteriolytic activities in the culture fluid of Myxococcus xanthus were purified and separated into six active fractions by the use of Bio-Gel CM-2 and Bio-Gel P-60. These fractions were identified as: (i) an amidase, (ii) a glucosaminidase, (iii) a glucosaminidase and an amidase, (iv) a protease with probable amidase activity, (v) another protease with probable amidase activity, and (vi) a peptidase active on both d-alanyl-diaminopimelate and d-alanyl-lysine peptide bonds. On one occasion, another amidase was eluted from Bio-Gel CM. Preliminary studies on some characteristics of the enzymes and their production during growth are reported.
利用Bio-Gel CM-2和Bio-Gel P-60对黄色粘球菌培养液中的溶菌活性进行了纯化,并分离成六个活性组分。这些组分被鉴定为:(i)一种酰胺酶,(ii)一种氨基葡萄糖苷酶,(iii)一种氨基葡萄糖苷酶和一种酰胺酶,(iv)一种可能具有酰胺酶活性的蛋白酶,(v)另一种可能具有酰胺酶活性的蛋白酶,以及(vi)一种对d-丙氨酰-二氨基庚二酸和d-丙氨酰-赖氨酸肽键均有活性的肽酶。有一次,从Bio-Gel CM上洗脱下来另一种酰胺酶。本文报道了对这些酶的一些特性及其在生长过程中产生情况的初步研究。