노랑초파리(Drosophila melanogaster)의 알코올 水素離脫酵素의 活性과 分離에 關한 硏究

A study on Activity and Separation of Alcohol Dehydrogenase in Drosophila melanogaster

  • 오석흔 (서울보건전문대학.위생과) ;
  • 정용재 (이화여대.과학교육과) ;
  • 박상윤 (성균관대.생물학과)
  • Oh, Suk Heun (Dept. of Sanitary Engineer, Seoul Health Junior College) ;
  • Chung, Yong Jae (Dept. of Science Education, Ewha Womans Univ.) ;
  • Park, Sang Yoon (Dept. of Biology, Sung Kyun Kwan Univ.)
  • 발행 : 1979.04.01

초록

Drosophila melanogaster Oregen-R을 大量飼育하여 alcohol dehydrogenase를 精製하여 그 活性을 測定하는 한편 alcohol dehydrogenase의 isozyme pattern을 分析한 結果 아래와 같은 몇가지 사실을 얻었다. 1. 본 실험을 통해서 Drosophila melanogaster Oregon-R의 alcohol dehydrogenase의 比活性은 Jacobson et al. (1970)이 報告한 바 있는 D. melanogaster Samarkands의 그것에 比하여 약 5배 이상의 比活性을 나타냄을 確認하였다. 2. 이 strain의 ADH isozyme pattern은 fast form인 $AHD_1, AHD_2$ 그리고 slow form인 $ADH_2$임을 알게 되었다. 3. 粗酵表에서의 ADH isozyme pattern은 $ADH_1, ADH_2$ 그리고 $ADH_5A$가 나타났는데, 정제효소에서는 $ADH_1, ADH_5A$$ADH_5B$가 나타났다. 4. $ADH_5A$$ADH_1$ isozyme을 分離 精製한 $ADH_5A$의 比活性은 4,330 units/mg이었고, $ADH_1$의 比活性은 3,670 units/mg임을 알게 되었으며, 이것을 7% acrylamide disc gel에 電氣泳動하여 zymogram의 位置를 정확히 판별하였다.

Drosophila melanogaster Oregon-R had been bred in a large quantity and the crude alcohol dehydrogenase (ADH) obtained was purified and the activity of the enzyme was measured, analyzed and its patterns were examined. The results obtained are presented below: 1. Through this experiment, it was found that the specific activity of ADH of the D. melanogaster is about more than five times as strong as that of the D. mlanogaster Samarkands which was found by Jacobson et al. in 1970. 2. It was learned that the ADH isozyme patterns of this strain was found to be $ADH_1$ and $AHD_2$ in the fast form and $ADH_5$ in the slow form. 3. It was learned that, $ADH_1, ADH_2$, and $ADH_5A$ are found as the ADH patterns of crude enzyme, and that $ADH_1, ADH_5A$ and $ADH_5B$ as the ADH patterns of the purified enzyme. 4. After the isolation andpurification of $ADH_5A$ and $ADH_1$ isozymes, specfic activity of $ADH_5A$ was found to be 4,330 (units/mg) and that of $ADH_1$ to be 3,670 (units/mg), and the exact position of their zymogram on the 7% acrylamide disc gel was distinguished.

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