自上世纪80年代核酮糖-1,5-二磷酸羧化酶/加氧酶活化酶(Ru Bis CO activase,RCA)被发现后,一直广受关注,其酶学特性、体内外活化及其对光合作用的影响、体内外活性调节机制、基因和分子结构、反义突变和超表达等研究,已成为了光合研究...自上世纪80年代核酮糖-1,5-二磷酸羧化酶/加氧酶活化酶(Ru Bis CO activase,RCA)被发现后,一直广受关注,其酶学特性、体内外活化及其对光合作用的影响、体内外活性调节机制、基因和分子结构、反义突变和超表达等研究,已成为了光合研究领域的一大热点。本文结合国内外研究进展,就RCA分子结构、与光合作用的关系,特别是其在植物抗逆中的作用等方面进行综述。展开更多
The degradation of Ribulose-1.5-bisphosphate carboxylase／oxygenase(Rubisco，EC4.1.1.39)in wheat(TnticumaestivumL．CV．Yan6mai 158)leaves dunng dark—induced senescence was studied．An／in vivo degradation product of ...The degradation of Ribulose-1.5-bisphosphate carboxylase／oxygenase(Rubisco，EC4.1.1.39)in wheat(TnticumaestivumL．CV．Yan6mai 158)leaves dunng dark—induced senescence was studied．An／in vivo degradation product of Rubisco large subunit(LSU)with molecular weiht of 50kD was detected by SDS—PAGE and immunobloted with antibody against tobacco Rubisco．This fragment could also be detected in natural senescence．The result also suggested that the Rubisco holoenzyme had not dissociated when LSU hydrolyzed from 53 kD to 50kD．And．LSUcould be fragmented to 50kD at 30-35℃and at DH7．5 in crude enzyme extracts of wheat leaves dark—induced for 48h．which suggested that maybe LSU was degraded to 50 kD by anunknown protease in chloroplast．展开更多
文摘自上世纪80年代核酮糖-1,5-二磷酸羧化酶/加氧酶活化酶(Ru Bis CO activase,RCA)被发现后,一直广受关注,其酶学特性、体内外活化及其对光合作用的影响、体内外活性调节机制、基因和分子结构、反义突变和超表达等研究,已成为了光合研究领域的一大热点。本文结合国内外研究进展,就RCA分子结构、与光合作用的关系,特别是其在植物抗逆中的作用等方面进行综述。
文摘The degradation of Ribulose-1.5-bisphosphate carboxylase／oxygenase(Rubisco，EC4.1.1.39)in wheat(TnticumaestivumL．CV．Yan6mai 158)leaves dunng dark—induced senescence was studied．An／in vivo degradation product of Rubisco large subunit(LSU)with molecular weiht of 50kD was detected by SDS—PAGE and immunobloted with antibody against tobacco Rubisco．This fragment could also be detected in natural senescence．The result also suggested that the Rubisco holoenzyme had not dissociated when LSU hydrolyzed from 53 kD to 50kD．And．LSUcould be fragmented to 50kD at 30-35℃and at DH7．5 in crude enzyme extracts of wheat leaves dark—induced for 48h．which suggested that maybe LSU was degraded to 50 kD by anunknown protease in chloroplast．
