Purification and Characterization of an Unusual Aminopeptidase From Pea Seeds
Keyword(s):
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.
1979 ◽
1992 ◽
Vol 267
(8)
◽
pp. 5374-5379
◽
1998 ◽
Vol 64
(2)
◽
pp. 789-792
◽
1998 ◽
Vol 64
(8)
◽
pp. 3029-3035
◽
1983 ◽
Vol 29
(10)
◽
pp. 1361-1368
◽
1979 ◽