
TY  - JOUR
A1  - Caldwell, JB 
A1  - Sparrow, LG 
T1  - Purification and Characterization of an Unusual Aminopeptidase From Pea Seeds
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 1980
VL  - 7
IS  - 2
SP  - 131
EP  - 140
KW  - 
UR  - https://doi.org/10.1071/PP9800131 
N2  - 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. 
ER  -

