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Studies on the purification of ACC synthase in tomato fruits

Hu Jiancheng, Hua Xuezeng, Liu Yu, Liang Houguo

Laboratory of Plant Physiology, Lanzhou University. Lanzhou 730000；China；Shanghai Institute of Plant Physiology, Chinese Academy of Sciences. Shanghai 200032

Abstract

The optimum time of incubation was found to be 10 h at 25℃ when the ACC synthase activity reached its maximum. Potassium phosphate buffer(PBP) and sodium phosphate buffer (PBS) showed the same effects on the extraction, but the reaction activity of the enzyme was twice as high in PBP as in PBS, indicating an activating effect of K~(+). PBP 100 mmol/L (pH 8.0, DTT 4 mmol/L, and PLP 5#mu#mol/L) was adopted as the extraction buffer. The use of polyethyleneglycol(PEG)6000(5%~13%)as the precipitant gave an ACC synthase activity twice as high as that of ammonium sulfate(40%~75%). The specific activity of ACC synthase was increased 7300 fold, reaching 116870 U/mg protein, and the yield was 7%. Purified ACC synthase showed a yellow strong band located at 50 kD after SDS-PAGE and silver staining. The amount of ACC synthase in tomato fruit pericarps induced by slicing was about 0.01% of the total soluble proteins.

Key words: Tomato fruit;ACC synthase;Purification

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Citing This Article：

Hu Jiancheng, Hua Xuezeng, Liu Yu, Liang Houguo. Studies on the purification of ACC synthase in tomato fruits. Acta Physiol Sin 1995; 47 (1): (in Chinese with English abstract).