Journal
PHYSIOLOGIA PLANTARUM
Volume 112, Issue 3, Pages 321-326Publisher
MUNKSGAARD INT PUBL LTD
DOI: 10.1034/j.1399-3054.2001.1120304.x
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A protease was isolated from potato (Solanum taberosum 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.
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