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PubMedDate not supplied

[Study of the pharmacokinetics of phosphemide in rats with the use of physico-chemical methods].

A study on the passage of phosphemide with urine and distribution of the drug over the organs and tissues of intact (without fumour) rats and those with sarcoma-45 showed the bulk of unchanged drug to be excreted together with the urine during the first 3-4 hours following its intravenous and intraperitoneal administration. In rats with sarcoma-45 phosphamide is passed with urine in a somewhat greater amount than in the intact animals. With intravenous application the rate of the drug elimination in intact rats and in the ones with carcoma-45 is virtually the same, being somewhat lower with intraperitoneal injection of phosphemide.

Animals↗
PubMed1975

Chemosterilant (apholate)-induced ultrastructural changes during oogenesis in Aedes aegypti.

The effect of chemosterilant, apholate, on-oogenesis has been studied in Aedes aegypti. Treatment of larvae to 20 ppm of the chemical induced ultrastural changes in the presumptive and primary follicles of the adult ovary. These changes comprised condensation of chromatin, disruption of nuclear envelope and extensive degeneration as evidenced by numerous myelin figures and residual bodies. In some primary follicles, where cellular degeneration was restricted to epithelial cells, no arrest in development was observed. However, in comparison with controls, these follicles also were retarded. Larval treatment with 30 ppm apholate completely supressed ovariolar development. High incidence of autophagy was observed in tissues at both dose levels.

Aedes↗
PubMed1975

Apholate.

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Animals↗
PubMed1964

TOXICITY OF METEPA TO RATS WITH NOTES ON TWO OTHER CHEMOSTERILANTS.

Although tepa, metepa, and apholate are only moderately toxic to rats by the oral route, the dermal toxicity of the first two is relatively high as compared with that of conventional insecticides. In the experiments reported, metepa caused no damage to the intestinal epithelium of rats, except following single doses in the fatal range. The organ primarily affected by repeated small doses of metepa is the testis; the ovaries and bone marrow are damaged only by higher dosage levels. Metepa at an oral dosage of 5 mg/kg/day (about 4% of the acute oral LD(50) level daily) produced severe reduction of fertility of male rats within 22 days, sterility within 70 days, and testicular atrophy within 77 days. Half that dosage produced a smaller reduction in fertility and only partial testicular atrophy in some rats within 197 days. Dosages of 1.25 mg/kg/day or less produced no detectable effect on fertility and no histological change in the testis in 197 days. The survival of newborn rats was not affected by any dosage given to their sires.

Administration, Oral↗
PubMed1992

Effects of lipids and detergents on the conformation of the nicotinic acetylcholine receptor from Torpedo californica.

The hydrophobic, photoreactive probe 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) was used to characterize the effects of lipids and detergents on acetylcholine receptor (AChR) conformation. Affinity purified AChR reconstituted into dioleoylphosphatidylcholine (DOPC), dioleoylphosphatidic acid (DOPA), and cholesterol showed the same pattern of [125I]TID-labeling and demonstrated the same reduction in labeling of all four subunits upon desensitization by the agonist carbamylcholine, as partially purified AChR in native lipids. On the basis of the patterns of [125I]TID incorporation, reconstitution into DOPC/DOPA also appeared to stabilize the resting (functional) conformation of the AChR, while reconstitution in DOPC/cholesterol or DOPC alone largely desensitized the AChR. The effects of lipids on the functional state of the AChR was determined independently by measuring the ability of AChR reconstituted into different lipid combinations to undergo the change in affinity for agonist diagnostic of desensitization. The dramatic reduction in the apparent levels of [125I]TID associated with the subunits of the AChR observed upon agonist-induced desensitization was shown not to be due to a change in affinity for tightly bound lipid. Solubilization of affinity purified AChR reconstituted into DOPC/DOPA/cholesterol by the non-ionic detergents octyl glucoside, Triton X-100, and Tween 20 (final detergent concentration = 1%) was shown to produce the same pattern of [125I]TID-labeling as desensitization by agonist, while solubilization in 1% sodium cholate appeared to stabilize a conformation of the AChR more similar to the resting state.

Affinity Labels↗
PubMed1992

Photoaffinity labeling of T4 endonuclease V with a substrate containing a phenyldiazirine derivative.

T4 endonuclease V recognizes thymine photodimers in DNA duplexes and, in a two-step reaction, cleaves the glycosyl linkage of the 5'-side thymidine and the phosphodiester linkage. To determine the amino acid residues responsible for binding thymine photodimers, a photoaffinity reagent, 4-(1-azi-2,2,2-trifluoroethyl)-benzoate, was linked to the aminoalkylphosphonate of a thymine photodimer in a 14-mer duplex. The reactive substrate was treated with the enzyme under UV light (365 nm). The nascent enzyme and the modified enzyme were treated with lysyl endopeptidase, and the peptide maps were compared. Three peptides from the C terminus were found to interact with the reactive oligonucleotide to various extents. The three modified peptides were isolated and analyzed by Edman degradation. The amino acid residues Gly-133, Tyr-129, and Thr-89 were partially linked with the reactive substrate and may be involved in the binding of thymine photodimers.

Affinity Labels↗
PubMed1992

Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist.

To characterize structural changes induced in the nicotinic acetylcholine receptor (AChR) by agonists, we have mapped the sites of photoincorporation of the cholinergic noncompetitive antagonist 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine (]125I]TID) in the presence and absence of 50 microM carbamylcholine. [125I]TID binds to the AChR with similar affinity under both these conditions, but agonist inhibits photoincorporation into all subunits by greater than 75% (White, B. H., Howard, S., Cohen, S. G., and Cohen, J. B. (1991) J. Biol. Chem. 266, 21595-21607). [125I]TID-labeled sites on the beta- and delta-subunits were identified by amino-terminal sequencing of both cyanogen bromide (CNBr) and tryptic fragments purified by Tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by reversed-phase high-performance liquid chromatography. In the absence of agonist, [125I]TID specifically labels homologous aliphatic residues (beta L-257, delta L-265, beta V-261, and delta V-269) in the M2 region of both subunits. In the presence of agonist, labeling of these residues is reduced approximately 90%, and the distribution of labeled residues is broadened to include a homologous set of serine residues at the amino terminus of M2. In the beta-subunit residues beta S-250, beta S-254, beta L-257, and beta V-261 are all labeled in the presence of carbamylcholine. This pattern of labeling supports an alpha-helical model for M2 with the labeled face forming the ion channel lumen. The observed redistribution of label in the resting and desensitized states provides the first direct evidence for an agonist-dependent rearrangement of the M2 helices. The efficient labeling of the resting state channel in a region capable of structural change also suggests a plausible model for AChR gating in which the aliphatic residues labeled by [125I]TID form a permeability barrier to the passage of ions. We also report increased labeling of the M1 region of the delta-subunit in the presence of agonist.

Amino Acid Sequence↗