| Literature DB >> 16666127 |
P Vera1, V Conejero.
Abstract
An endoproteinase induced by citrus exocortis viroid has been purified from tomato (Lycopersicon esculentum Mill, cv "Rutgers") leaves. The proteinase corresponds to one of the major pathogenesis-related proteins of tomato plants and was designated proteinase P-69 as it has a molecular weight of 69,000 to 70,000. The proteinase was purified in four steps: (NH(4))(2)SO(4) fractionation, chromatography on Bio-Gel P-60, DEAE-Sepharose chromatography, and casein-Sepharose affinity chromatography. The proteinase had a pH optimum of 8.5 to 9.0 when assayed with either fluorescein thiocarbamoyl derivative (FTC)-casein or FTC-ribulose 1,5-bisphosphate carboxylase/oxygenase as substrates. The proteinase activity was inhibited by pCMB and strongly activated by calcium and magnesium ions as well as by DTT. When analyzed by electrofocusing, the activity showed a pI around 9.0.Entities:
Year: 1988 PMID: 16666127 PMCID: PMC1054699 DOI: 10.1104/pp.87.1.58
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340