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. 1988 Dec;85(23):8810–8814. doi: 10.1073/pnas.85.23.8810

Identification of a unique isoform of 1-aminocyclopropane-1-carboxylic acid synthase by monoclonal antibody

Arkesh M Mehta 1, Ramon L Jordan 1, James D Anderson 1, Autar K Mattoo 1,*
PMCID: PMC282596  PMID: 16593998

Abstract

1-Aminocyclopropane-1-carboxylic acid (ACC) synthase (EC 4.4.1.14) is a key enzyme regulating ethylene biosynthesis in higher plants. A monoclonal antibody (mAb T20C) that immunoprecipitates the ACC synthase activity from tomato pericarp tissue extracts revealed that mAb T20C immunodecorates an ≈67-kDa polypeptide. On isoelectric focusing gels, ACC synthase activity in cell-free preparations was resolved into three distinct activity peaks with pI values 5.3, 7, and 9. mAb T20C specifically recognized the pI 7 form of the enzyme on electrophoretic transfer (Western) blots. When analyzed by sodium dodecyl sulfate gel electrophoresis under reducing conditions, the eluted pI 7 form was confirmed to migrate as a polypeptide of 67 kDa. The 67-kDa pI 7 isoform is a previously undescribed form of ACC synthase.

Keywords: ethylene, 1-aminocyclopropane-1-carboxylic acid synthase, hormones, Lycopersicon esculentum L.

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