Author:
Sullivan JJ,Muchnicky EE,Davidson BE,RJago G
Abstract
Pyrrolidonecarboxylate peptidase (BC 3.4.11.8) from Streptococcus faecium was purified by fractionation with streptomycin sulphate and ammonium sulphate, by chromatography on Sephadex G200 and DBAB-cellulose, and by preparative electrophoresis on Sephadex G25. The purified enzyme on acrylamide gel showed a strong protein band which contained enzyme activity and a very faint band which had no activity.
Subject
Developmental Biology,Endocrinology,Genetics,General Materials Science,Molecular Biology,Animal Science and Zoology,Reproductive Medicine,General Medicine,Biotechnology
Cited by
18 articles.
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