Purification and characterization of an aspartic protease from potato leaves

A protease was isolated from potato (Solanum tuberosum L. cv. Pampeana) leaves 48 h after detaching, when aspartic protease (AP) activity is markedly increased. Purification was performed by ammonium sulfate precipitation, ion exchange chromatography and affinity chromatography. A size of 40 kDa was...

Full description

Saved in:
Bibliographic Details
Published in:Physiologia plantarum 2001-07, Vol.112 (3), p.321-326
Main Authors: Guevara, María G., Daleo, Gustavo R., Oliva, Claudia R.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Enzymes
Fundamental and applied biological sciences. Psychology
Metabolism
Plant physiology and development
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A protease was isolated from potato (Solanum tuberosum L. cv. Pampeana) leaves 48 h after detaching, when aspartic protease (AP) activity is markedly increased. Purification was performed by ammonium sulfate precipitation, ion exchange chromatography and affinity chromatography. A size of 40 kDa was estimated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis; it is monomeric and its properties are consistent with those of aspartic proteinases (EC 3.4.23): it has a pH optimum of 3 and it is inhibited by pepstatin. Like other plant APs, leaf AP appears to be glycosylated with a complex‐type N‐glycan. The enzyme has properties different from those of a tuber AP previously described, indicating that they may have different physiological roles.
ISSN:0031-9317
1399-3054
DOI:10.1034/j.1399-3054.2001.1120304.x