Premium
Purification and characterization of an aspartic protease from potato leaves
Author(s) -
Guevara María G.,
Daleo Gustavo R.,
Oliva Claudia R.
Publication year - 2001
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.2001.1120304.x
Subject(s) - pepstatin , ammonium sulfate precipitation , protease , chromatography , polyacrylamide gel electrophoresis , gel electrophoresis , biochemistry , solanum tuberosum , affinity chromatography , chemistry , glycan , aspartic acid , ion chromatography , ammonium sulfate , sodium dodecyl sulfate , enzyme , biology , botany , amino acid , size exclusion chromatography , glycoprotein
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.