Pathogenesis-Related Proteins of Tomato | Zendy

Pablo Vera | Zendy; Vicente Conejero | Zendy

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Pathogenesis-Related Proteins of Tomato

Author(s) -

Pablo Vera,

Vicente Conejero

Publication year - 1988

Publication title -

plant physiology

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.87.1.58

Subject(s) - affinity chromatography , biochemistry , sepharose , casein , lycopersicon , ion chromatography , isoelectric focusing , chemistry , pathogenesis related protein , solanaceae , chromatography , biology , enzyme , botany , gene

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.

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