首页> 外文OA文献 >Effects of Exogenous 1,3-Diaminopropane and Spermidine on Senescence of Oat Leaves 1: I. Inhibition of Protease Activity, Ethylene Production, and Chlorophyll Loss as Related to Polyamine Content
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Effects of Exogenous 1,3-Diaminopropane and Spermidine on Senescence of Oat Leaves 1: I. Inhibition of Protease Activity, Ethylene Production, and Chlorophyll Loss as Related to Polyamine Content

机译:外源1,3-二氨基丙烷和亚精胺对燕麦叶片1衰老的影响:I。蛋白酶活性,乙烯的产生以及与多胺含量相关的叶绿素损失的抑制

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摘要

Excision and dark incubation of oat (Avena sativa L., var. Victory) leaves cause a sharp increase in protease activity, which precedes Chl loss. Both these senescence processes are inhibited by exogenously applied 1,3-diaminopropane (Dap), which occurs naturally in leaf segments. The inhibition of protease activity is much greater in vivo than in vitro, suggesting inhibition of protease synthesis as well as protease action by Dap. Chl breakdown in leaves of radish and broccoli, which also senesce rapidly in the dark, is only slightly inhibited by DaP. These differences between cereal and dicotyledonous plants are correlated with the natural occurrence of Dap in cereals. In the light, Dap promotes, rather than retards, the loss of Chl in oat leaves. This resembles previously described effects of other polyamines. Addition of Mg2+ to the medium does not antagonize this effect. In the dark, the accumulated Dap also inhibits ethylene production and decreases titer of other polyamines. Addition of Ca2+ to the incubation medium containing Dap competitively reduces the effects of Dap. Thus, Dap, like other polyamines, seems to require an initial attachment to a membrane site shared with Ca2+ before exerting its antisenescence action.
机译:燕麦叶片的切除和黑暗孵育会导致蛋白酶活性急剧增加,这是在Chl丧失之前。这两个衰老过程均受到外源施加的1,3-二氨基丙烷(Dap)的抑制,后者自然发生在叶片中。体内对蛋白酶活性的抑制比体外要大得多,表明对蛋白酶合成的抑制以及Dap的蛋白酶作用。萝卜和西兰花叶片中的Chl分解,在黑暗中也会迅速衰老,而DaP只能抑制这种现象。谷物和双子叶植物之间的这些差异与谷物中Dap的天然存在相关。鉴于此,Dap促进而不是阻碍了燕麦叶片中Chl的损失。这类似于先前描述的其他多胺的作用。向介质中添加Mg2 +不会拮抗这种作用。在黑暗中,积累的Dap也会抑制乙烯的产生并降低其他多胺的滴定度。向含有Dap的孵育培养基中添加Ca2 +会竞争性地降低Dap的作用。因此,与其他多胺一样,Dap似乎需要在与Ca2 +共享的膜部位上进行初始附着,然后再发挥其抗衰老作用。

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