Ota A
Department of Biochemical Sciences, Frick Chemical Laboratory, Princeton University, New Jersey 08540.
Microbios. 1993;75(302):33-8.
The pH dependency of a Co(2+)-dependent dipeptidase from Escherichia coli AJ005, a peptidase-deficient mutant strain K12, was examined with purified dipeptidase, which was about 106-fold in specific activity. The peptidase had a very sharp optimal pH at 7.5. It is suggested that the peptidase plays an important role in the process of cell division and growth.
对来自大肠杆菌AJ005（一种肽酶缺陷型突变菌株K12）的钴（2+）依赖性二肽酶的pH依赖性进行了研究，使用的是比活性约为106倍的纯化二肽酶。该肽酶在pH 7.5时具有非常尖锐的最佳pH值。据推测，该肽酶在细胞分裂和生长过程中起重要作用。
