
%0 Journal Article
%A Sullivan, JJ 
%A Muchnicky, EE 
%A Davidson, BE 
%A RJago, G 
%T Purification and Properties of the Pyrrolidonecarboxylate Peptidase of Streptococcus faecium
%J Australian Journal of Biological Sciences
%D 1977/12/01
%V 30
%N 6
%P 543-552
%K 
%R https://doi.org/10.1071/BI9770543
%U https://www.publish.csiro.au/paper/BI9770543 
%X 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. 
