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| 題 名 | Evidence for Arylamine N-Acetyltransferase in Hymenolepis Nana=短小包膜絛虫發現含有N-乙醯轉移酵素 |
|---|---|
| 作 者 | 鍾景光; 郭秀滿; 吳禮字; 賴建銘; 李昭宏; 洪啟賦; | 書刊名 | 中華民國微生物及免疫學雜誌 |
| 卷 期 | 30:1 1997.02[民86.02] |
| 頁 次 | 頁1-17 |
| 分類號 | 415.121 |
| 關鍵詞 | 短小包膜絛虫; N-乙醯轉移酵素; 2-aminofluorene; N-acetyl-2-aminofluorene; N-acetyltransferase; P-aminobenzoic acid; N-acetyl-p-aminobenzoic acid; Hymenolepis nana; |
| 語 文 | 英文(English) |
| 中文摘要 | 老鼠腸內分離出的短小包膜絛虫經萃取而利用p-aminobenzoic acid及2-amin ofluorene當作受質,證實含有N- 乙醯轉移酵素的活性存在。此酵素活性可經乙醯輔助酵素作為乙醯基的提供者而經由高壓液相層析儀來證實。由50隻短小包膜絛虫組織萃取而得N-乙醯轉移酵素的活性以p-aminobenzoic acid為受質其酵素催化力是2.83 ± 0.31 nmol/min/mg protein。若以2-aminofluorene為受質則其酵素催化力是2.07 ± 0.24 nmol/min/mg protein。若以2-aminofluorene為受質其Km值為1.06 ± 0.38 mM, Vmax為8.92 ± 1.46 nmol/min/mg protein。而以p-aminobenzoic acid為受質其Km值則為2.16 ± 0.19 mM, Vmax為12.68 ± 2.26 nmol/min/mg protein。此酵素反應的最適pH酸鹼值為8.0,最適宜的反應溫度為38 °C,此酵素亦受iodacetamide的抑制,當iodacetamide濃度增加時,其抑制作用亦增強。蛋白質酵素抑制劑中iodoacetate也可抑制此酵素的作用,二價離子中的鐵、鈣及鋅離子也能抑制此酵素的活性,這是第一次證明絛虫綱中的短小包膜絛蟲存在N- 乙醯轉移酵素。 |
| 英文摘要 | N-acetyltransferase activities with p-aminobenzoic acid and 2-aminofluo rene were determined in Hymenolepis nana, a cestode found in the intestine of the Sprague-Dawley rats. The N-acetyltransferase activity was determined using an acetyl CoA recycling assay and high pressure liquid chromatography. The N-acety ltransferase activities from a number of Hymenolepis nana whole tissue homogenizations were found to be 2.83 ± 0.31 nmole/min/mg for 2-aminofluorene and 2.07 ± 0.24 nmole/min/mg for paminobenzoic acid. The apparent Km and Vmax were 1.06 ± 0.38 mM and 8.92 ± 1.46 nmol/min/mg for 2-aminofluorence, and 2.16 ± 0.19 mM and 12.68 ± 2.26 nmol/min/mg for p-aminobenzoic acid. The optimal pH value for the enzyme activity was pH 8.0 for both substrates tested. The optimal temperature for enzyme activity was 37 °C for both substrates. The N-acetyltransferase activity was inhibited by iodacetamide. At 0.25 mM iodacetamide the activity was reduced 50% and 1.0 mM iodacetamide inhibited activity more than 90%. Among a series of divalent cations and salts, Fe����, Ca���� and Zn���� wer demonstrated to be the most potent inhibi-tors. Among the protease inhibitors, only ethylenediamineteraacetic acid significantly protected N-acetyltransferase. Iodoacetate, in contrast to other agents, markedly inhibited N-acetyltransferase activity. This is the first demonstration of acetyl CoA:arylamine N-acetyltransferase activity in a cestode and extends the number of phyla in which this activity has been found. |
本系統中英文摘要資訊取自各篇刊載內容。