以硬溶质型桃果实‘加纳岩’为试材,研究外源乙烯处理对桃果实采后贮藏过程中呼吸速率、乙烯释放量、细胞色素氧化酶(cytochrome C oxidase,COX)活性以及线粒体编码的COX 3种亚基(COXⅠ、COXⅡ、COXⅢ)基因表达量的影响。结果表明:外源...以硬溶质型桃果实‘加纳岩’为试材,研究外源乙烯处理对桃果实采后贮藏过程中呼吸速率、乙烯释放量、细胞色素氧化酶(cytochrome C oxidase,COX)活性以及线粒体编码的COX 3种亚基(COXⅠ、COXⅡ、COXⅢ)基因表达量的影响。结果表明:外源乙烯处理加速了硬溶质型桃果实‘加纳岩’在采后贮藏过程中硬度的下降,促进了呼吸作用和内源乙烯释放,使呼吸高峰和乙烯释放高峰提前出现。同时外源乙烯抑制了COX酶活性,抑制了贮藏后期COXⅠ和COXⅡ亚基基因的表达,抑制了整个贮藏过程中COXⅢ亚基基因的表达。外源乙烯处理抑制了COX途径的呼吸,加速了果实的软化衰老。展开更多
The fluorescence quenching spectra of the holo-Cu A and apo-Cu A domain of cytochrome c oxidase from Para coccus versutus by KI were investigated.The results indicated that in solution part of the fluorophore tryptoph...The fluorescence quenching spectra of the holo-Cu A and apo-Cu A domain of cytochrome c oxidase from Para coccus versutus by KI were investigated.The results indicated that in solution part of the fluorophore tryptophanes of the Cu A domain are exposed to the surface of the protein,and others buried inside o f the hydrophobic core.The fluorescence quenching constants of holo-Cu A and apo-Cu A domain protein by KI are1.39and2.24,respectively,which suggested t hat the bi-nuclear copper center[Cu A+1.5 -Cu A+1.5 ]also plays a role on the structural stability of the protein.展开更多
文摘以硬溶质型桃果实‘加纳岩’为试材,研究外源乙烯处理对桃果实采后贮藏过程中呼吸速率、乙烯释放量、细胞色素氧化酶(cytochrome C oxidase,COX)活性以及线粒体编码的COX 3种亚基(COXⅠ、COXⅡ、COXⅢ)基因表达量的影响。结果表明:外源乙烯处理加速了硬溶质型桃果实‘加纳岩’在采后贮藏过程中硬度的下降,促进了呼吸作用和内源乙烯释放,使呼吸高峰和乙烯释放高峰提前出现。同时外源乙烯抑制了COX酶活性,抑制了贮藏后期COXⅠ和COXⅡ亚基基因的表达,抑制了整个贮藏过程中COXⅢ亚基基因的表达。外源乙烯处理抑制了COX途径的呼吸,加速了果实的软化衰老。
文摘The fluorescence quenching spectra of the holo-Cu A and apo-Cu A domain of cytochrome c oxidase from Para coccus versutus by KI were investigated.The results indicated that in solution part of the fluorophore tryptophanes of the Cu A domain are exposed to the surface of the protein,and others buried inside o f the hydrophobic core.The fluorescence quenching constants of holo-Cu A and apo-Cu A domain protein by KI are1.39and2.24,respectively,which suggested t hat the bi-nuclear copper center[Cu A+1.5 -Cu A+1.5 ]also plays a role on the structural stability of the protein.
