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題 名 | Isolation and Characterization of a Group Ⅲ Isozyme of Acid Phosphatase from Rice Plants=水稻的酸性燐酸酵素的純化與鑑定 |
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作 者 | 左士嘉; 陳榮銳; | 書刊名 | Botanical Bulletin of Academia Sinica |
卷 期 | 38:4 1997.10[民86.10] |
頁 次 | 頁245-250 |
分類號 | 434.113 |
關鍵詞 | 酸性燐酸酵素; 同功酵素; 純化; 水稻; Acid phosphatase; Enzyme purification; Isozyme; Oryza sativa; |
語 文 | 英文(English) |
中文摘要 | 水稻幼苗含四組酸性燐酸酵素同功酵素。經硫酸銨沈澱、DEAE-Sepharose, Con A-Sepharose 及 Chromatofocusing 等法純化所得的第三組同功酵素, 其活性增高至 198 倍。 以膠體過濾色層分析分離鑑定有兩帶,其分子亮分別為 130 kDa 及 100 kDa,然而在 native-PAGE 上只呈一帶。其最適酸鹼度在五左右,對 p-Nitrophenyl phosphate (p-NPP) 的 Km 值是 0.33 mM。氟化鈉對本組酵素的抑制作用屬非競爭性效應。氯化汞、鉬酸鈉及硫 酸銅對酵素活性有很強的抑制性。本組同功酵素對 ATP 及 p-NPP 有很強的水解效果,且可 部分解水 Fructose-1, 6-diphosphate, 至於 Fructose-6-phosphate, Glucose-1-phosphate, Glucose-6-phosphate, Glycerophophosphate 及 Adenosine monophosphate 則非為受質。 |
英文摘要 | The acid phosphatases (EC 3. 1. 3. 2.) of rice seedlings consisted of four groups of isozymes. The group Ⅲ isozyme was purified through ammonium sulfate, DEAE-Sepharose, Con A-Sepharose, and chromatofocusing. A 198-fold enhancement of activity was attained. This isozyme showed only one band in native-polyacryamide gel electrophoresis. However, gel filtration revealed two peaks of enzyme activity. Their molecular weights were 130 kDa and 100 kDa. The purified isozyme showed a pH optimum of 5. Its Km for p-nitrophenyl phosphate (p-NPP) hydrolysis was 0.33 mM. Its activity was inhibited non-competitively by sodium fluoride. Mercuric chloride, sodium molybdate, and copper sulfate strongly inhibited the enzyme activity. The isozyme actively hydrolyzed adenosine triphosphate and p-NNP, and partially utilized fructose-1, 6-diphosphate. It did not utilize fructose-6-phosphate, glucose-1-phosphate, glucose-6-phosphate, glycerophosphate, or adenosine monophosphate. |
本系統中英文摘要資訊取自各篇刊載內容。