摘要
本文报告了满江红（Ａｚｏｌｌａｉｍｂｒｉｃａｔａ）多胺氧化酶特性的一些研究结果。该酶的最适底物为ｓｐｄ（亚精胺），其次为ｓｐｍ（精胺）（酶活性约为以ｓｐｄ为底物时的４０％），而对ｐｕｔ（腐胺）和ｃａｄ（尸胺）两种二胺几乎不氧化；在５０—７０℃或ｐＨ４—１０的范围内均有活性，以ｓｐｄ和ｓｐｍ作底物时的最适ｐＨ值分别为６．５和５．５；该酶经１０ｍｍｏｌ／Ｌ的ＥＤＴＡ处理后酶活性仍能完全保持，说明其催化功能的实现可能无需金属离子的参与。另外，金属离子Ｃａ￣（２＋）、Ｍｇ￣（２＋）对该酶活性无明显影响，但１０ｍｍｏｌ／Ｌ的ＣｕＳＯ＿４可抑制约２０％的活性。
A study on the properties of polyamine oxidase( PAO)from Azolla imbricatashowed :(1) The PAO was quite stable when exposed to high temperature(50 70℃);(2)The optimum substrate for PAO is spermidine(spd).and secondly speimine(spm), PAO’s ac-tivity was about 40 % of that while spd was used as substrate.The PAO showed no detectiveactivity with putrescine or cadaverine as substrate;(3) Its optimum pH was 6.5 and 5. 5 withspd and spm as substrate respectively;(4) It is considered that metal ion may be not necessaryfor its catalytic activity since 10 mmol/L EDTA(ethylene diaminetetra acetic acid) had no in-hibitive effect on the enzyme. Metal ions Ca￣(2+),Mg￣(2+) also had no detective effect on the en-zyme, while 10 mmol/L CuSO_4 inhibited its activity by about 20%.
出处
《仲恺农业技术学院学报》
1996年第2期60-64,共5页
Journal of Zhongkai Agrotechnical College
基金
国家教委博士点基金
