Insect epoxide hydrolase: Properties of a purified enzyme from the southern armyworm (Spodoptera eridania)

An epoxide hydrolase purified from midgut microsomes of southern armyworm (Spodoptera eridania) larvae exhibited high activity toward monosubstituted epoxides (1,2-epoxyoctane, 1,2-epoxypropane, and styrene oxide) and lower activity toward cis-1,2-disubstituted epoxides (cyclohexene oxide, and the cyclodienes HEOM, HCE, and chlordene epoxide). Trisubstituted epoxides (2-methyl-2,3-epoxyheptane and JH-1) as well as several cyclodiene insecticides (dieldrin, endrin, endo-epoxyaldrin, and anti-heptachlor epoxide) were refractory to enzymatic attack. It is concluded that both lipophilic and steric factors dictate the substrate specificity of the enzyme. With cyclohexene oxide the enzyme yields the 1R, 2R enantiomer of the trans-diol. The purified enzyme is inhibited by several epoxides and mixed-function oxidase inhibitors and the potency of 3,3,3-trichloro-1,2-epoxypropane and sodium picrylsulfonate suggest the importance of electronic factors in the inhibitory mechanism. Studies with specific amino acid modifiers suggest the presence of an essential lysine or histidine residue at the active site and indicate that the enzyme lacks a metal ion requirement and an essential cysteine residue. The purified enzyme has a molecular weight of 46,000 daltons and amino acid analysis and immunochemical studies show it to be very similar to, but not identical with, the epoxide hydrolase from mammalian liver microsomes.     

Localizing the action of two thiadiazolyl herbicidal derivatives

Enzymatically isolated leaf cells from navy beans (Phaseolus vulgaris L., cv. “Tuscola”) were used to study the effect of buthidazole (3-[5-(1,1-dimethylethyl)-1,3,4-thiadiazol-2-yl]-4-hydroxy-1-methyl-2-imidazolidinone) and tebuthiuron (N-[5-(1,1-dimethylethyl)-1,3,4-thiadiazol-2-yl]-N,N′-dimethylurea) on photosynthesis, protein, ribonucleic acid (RNA), and lipid synthesis. The incorporation of NaH¹⁴CO₃, [¹⁴C]leucine, [¹⁴C]uracil, and [¹⁴C]acetic acid as substrates for the respective metabolic process was measured. Time-course and concentration studies included incubation periods of 30, 60, and 120 min and concentrations of 0.1, 1, 10, and 100 μM of both herbicides. Photosynthesis was very sensitive to both buthidazole and tebuthiuron and was inhibited in 30 min by 0.1 μM concentrations. RNA and lipid syntheses were inhibited 50 and 87%, respectively, by buthidazole and 42 and 64%, respectively, by tebuthiuron after 120 min at 100 μM concentration. Protein synthesis was not affected by any herbicide at any concentration or any exposure time period. The inhibitory effects of buthidazole and tebuthiuron on RNA and lipid syntheses may be involved in the ultimate herbicidal action of these herbicidal chemicals.     

The relationship between the pharmacokinetics of intravenous cismethrin and bioresmethrin and their mammalian toxicity

The distribution and excretion of [¹⁴C]alcohol-labeled cismethrin and bioresmethrin was determined after intravenous administration to rats. Initially the label distribution of both isomers was similar, but differences occurred at later times mainly due to the retention of 5-benzyl-3-furylcarboxylic acid, a metabolite of bioresmethrin, in high concentration in the blood. Retention of this metabolite accounted for the slower excretion of bioresmethrin label compared to cismethrin. After administration of either isomer, parent pyrethroid was rapidly cleared from the blood and liver, and both isomers rapidly entered the central nervous system reaching peak concentrations within 2–5 min. Brain cismethrin concentrations exceeding 3.5 nmol/g were associated only with animals showing tremors. These levels of cismethrin are maintained for up to 30 min but bioresmethrin was depleted more rapidly possibly due to brain metabolism. It is concluded that the low toxicity of bioresmethrin is possibly due to the inability of this isomer to interact with the site of action in the central nervous system and not, as previously suggested, primarily because of more rapid metabolism in the liver.     

Homoeologous chromosome pairing: frequency differences in inbred and intraspecific hybrid polyploid ferns

The homosporous fern Ceratopteris thalictroides (Parkeriaceae) has evolved a polyploid genetic system that serves to store and release genetic variability in spite of self-fertilization and Mendelian homozygosity. This is demonstrated by the segregation of a gametophyte mutant within two inbred tetraploid lines and in their intraspecific hybrid. The segregation behavior can be explained by a model involving a duplicated locus and regular homoeologous chromosome pairing. Homoeologous pairing occurs at low levels in the inbred lines and at a high level in the hybrid, indicating intraspecific differences in chromosome pairing affinities.