摘要
采用琼脂法与整株法测定黑龙江省玉米田12种稗草生物型对莠去津、乙草胺和硝磺草酮抗性水平,同时测定不同抗性生物型体内SOD、POD、CAT及GSTs酶活性变化差异。结果表明,宾县生物型对莠去津产生低水平抗性,抗性指数为5.01。鸡西和五常生物型抗性指数分别为3.40和3.23,处于敏感性下降阶段。12种稗草生物型对乙草胺和硝磺草酮均未产生抗性;施用莠去津0~11 d,宾县生物型体内GSTs酶活性变化率始终高于五常和敏感生物型,3 d后POD酶活性变化率开始显著高于敏感生物型,其酶活性平均变化率与稗草抗性水平呈正相关;SOD和CAT酶活性变化率与稗草对莠去津抗性程度无关。稗草产生抗性可能是体内GSTs对莠去津代谢作用加强所致,与POD酶活性变化有关。
The resistances of 12 biotypes of Echinochloa crusgalli(L.)Beauv in corn field in Heilongjiang Province to atrazine,acetochlor and mesotrione were determined by agar method and whole plant method.Meanwhile,the enzyme activities of SOD,POD,CAT and GSTs in different biotypes were studied.The results showed that the biotype of Binxian county had a low level of resistance to atrazine,and the resistant index was 5.01.The biotypes of Jixi and Wuchang cities were in the stage of decreased sensitivity,resistant indice were 3.40 and 3.23,respectively.The resistance of 12 biotypes to acetochlor and mesotrione was not detected.The change rate of GSTs enzyme activity in Binxian county biotype was always higher than that of Wuchang city and sensitive biotypes from 0 d to 11 d.After 3 d,the change rate of POD activity began to be significantly higher than that of sensitive biotypes,and the average change rate of enzyme activity was positively correlated with the resistance level of barnyardgrass.The change rates of enzyme activities of SOD and CAT were not related to the resistance of Echinochloa crusgalli(L.)Beauv to atrazine.Resistance to Echinochloa crusgalli(L.)Beauv may be due to enhanced in vivo metabolism of atrazine by GSTs,and may be related to change in POD enzyme activity.
作者
刘亚光
唐兴佳
刘蓝坤
朱金文
张建树
LIU Yaguang;TANG Xingjia;LIU Lankun;ZHU Jinwen;ZHANG Jianshu(School of Agriculture,Northeast Agricultural University,Harbin 150030,China;School of Agriculture and Biotechnology,Zhejiang University,Hangzhou 310029,China)
出处
《东北农业大学学报》
CAS
CSCD
北大核心
2018年第4期29-39,共11页
Journal of Northeast Agricultural University
基金
国家重点研发计划项目(2017YFD0200307)
关键词
稗草
除草剂
抗性
酶活性
Echinochloa crusgalli(L.)Beauv
herbicide
resistance
enzyme activity