Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbicide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Nontreated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pretreatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metolachlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreatment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of glutathione S-transferase activity in etiolated maize shoots, and the selective enhancement of glutathione S-transferase isozymes by the safener CGA -154281.
Selective Enhancement of Electrochemical Signal Based on the Size of Alcohols Using Nanoporous Platinum
