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豇豆多胺氧化酶的底物动力学研究 被引量:1

Substrate Kinetics of Polyamine Oxidase from Vigna unguiculata
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摘要 从豇豆(Vigna unguiculata) 幼叶分离纯化的多胺氧化酶对腐胺(Put)、尸胺(Cad)、1,6-己二胺和1,IO-癸二胺等二胺类底物有较强的亲和力,底物的碳链长度越短,亲和力越强.该酶对亚精胺(Spd)和精胺(Spm)的氧化也有一定的催化活性.另外,反应介质的[Spd]/和[Spm]/[Put]比值以及O2浓度对该酶的催化活性有调节作用. Polyamine oxidase purified from Vigna unguiculata primary leaves could catalyze oxidation of polyamines such as putrescine (Put), cadaverine (Cad), spemiidine (Spd) and speimine (Spm), but its effective substrates were diamines. It appeared that the enzyme was more specific for short chain diamines than for longer chain ones. The enzyme activity was regulated by [Spd] / [Put] or [Spm] / [Put] ratio in the reaction medium. It had no activity if the oxygen concentration in the re- action medium was below 20 μmol/L, but the activity increased rapidly when oxygen concentration in- creasing from 25 to 80 μmol/L, then kept constant.
出处 《中山大学学报(自然科学版)》 CAS CSCD 北大核心 2000年第z2期119-122,共4页 Acta Scientiarum Naturalium Universitatis Sunyatseni
基金 国家教委博士点基金资助项目(9455808) 广东省自然科学基金资助项目(970655)
关键词 豇豆(Vigna unguiculata) 多胺氧化酶 多胺 底物动力学 diamine oxidase polyamine oxidase substrate kinetics Vigna unguiculata
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