Beltsville Agricultural Research Center, U.S. Department of Agriculture, Agricultural Research Service, Beltsville, MD 20705.
Proc Natl Acad Sci U S A. 1988 Dec;85(23):8810-4. doi: 10.1073/pnas.85.23.8810.
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 approximately 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.
1-氨基环丙烷-1-羧酸（ACC）合酶（EC 4.4.1.14）是调节高等植物中乙烯生物合成的关键酶。一种从番茄果皮组织提取物中免疫沉淀 ACC 合酶活性的单克隆抗体（mAb T20C）表明，mAb T20C 免疫标记了大约 67 kDa 的多肽。在等电聚焦凝胶上，无细胞制剂中的 ACC 合酶活性被解析为具有 pI 值 5.3、7 和 9 的三个不同活性峰。mAb T20C 特异性地在电泳转移（Western）印迹上识别酶的 pI 7 形式。当在还原条件下用十二烷基硫酸钠凝胶电泳分析时，洗脱的 pI 7 形式被确认为迁移为 67 kDa 的多肽。67 kDa pI 7 同工型是以前未描述的 ACC 合酶形式。
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