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．
