Frère J M, Moreno R, Ghuysen J M
Biochem J. 1974 Oct;143(1):233-40. doi: 10.1042/bj1430233.
The exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase-transpeptidase from Streptomyces R61.
来自链霉菌R39的细胞外双功能羧肽酶-转肽酶被纯化至蛋白质均一且达到毫克量。分离出的酶由一条分子量约为53300的多肽链组成。测定了其氨基酸组成和若干理化性质,并与来自链霉菌R61的细胞外双功能羧肽酶-转肽酶进行了比较。