
%0 Journal Article
%A Caldwell, JB 
%A Sparrow, LG 
%T Purification and Characterization of an Unusual Aminopeptidase From Pea Seeds
%J Functional Plant Biology
%D 1980/04/01
%V 7
%N 2
%P 131-140
%K 
%R https://doi.org/10.1071/PP9800131
%U https://www.publish.csiro.au/paper/PP9800131 
%X An aminopeptidase with specificity for N-terminal glutamic and aspartic acid residues has been purified to apparent homogeneity from pea seeds (Pisum sativum cv. Greenfeast). It also catalyses the hydrolysis of the glutaryl-phenylalanine bond of the synthetic chymotrypsin substrate glutaryl- L-phenylalanine p-nitroanilide. The native enzyme, which has a molecular weight of approximately 500 000, gives a single band on polyacrylamide gel electrophoresis but two major bands when subjected to electrophoresis in the presence of sodium dodecyl sulfate after reduction. Its behaviour with various inhibitors suggests that a sulfhydryl group is important for its activity. 
