Studies of hog kidney acylase I. I. Comparison with hog kidney dialkylfluorophosphatase.

Hog kidney Acylase I, an enzyme which hydrolyzes N-acetylL-amino acids, has been purified approximately 40-fold by Greenstein (1). During the course of the purification of hog kidney dialkylfluorophosphatase, it was consistently found that the protein fractions containing DFPasel activity also possessed very high Acylase I activity. Inasmuch as the DFPase and Acylase I activities were found to possess a number of similar properties and separation of the two activities was not effected in the early fractionation studies, the suggestion was advanced that a single enzyme might be responsible for both activities (2). However, further purification of the hog kidney fractions has resulted in a considerable degree of separation of the two enzymatic activities. In the present report, data are presented which distinguish between the enzymes and contradict the belief in their identity previously supported by one of the authors (2).