Detail of "4117-14-0"

Reference

Synthesis of acetates of 2(E)-hexenol, 2(E)-octenol and 2(E)-decenol

Synthesis of acetates of 2(E)-hexenol, 2(E)-octenol and 2(E)-decenol.Some chemicals with cas registry numbers like 4117-14-0 and 110-53-2 are also used. Vig, O. P.; Jindal, R. T. (Dep. Chem., Panjab Univ., Chandigarh 160 014, India). Indian J. Chem., Sect. B, 22B(9), 919-20 (English) 1983. CODEN: IJSBDB. ISSN: 0376-4699. DOCUMENT TYPE: Journal CA Section: 26 (Biomolecules and Their Synthetic Analogs) The sex attractants (E)=RCH:CHCH2OAc (I, R = Pr, pentyl, heptyl) were synthesized. Selective C-alkylation of propargyl alc. with RBr yields RCYCCH2OH. Redn. of the acetylenic bonds with LiAlH4 and acetylation gave I. .

Depletion of rat hepatic glutathione and inhibition of microsomal trans-2-enoyl-CoA reductase activity following administration of a dec-2-ynol and dec-2-ynoic acid

Depletion of rat hepatic glutathione and inhibition of microsomal trans-2-enoyl-CoA reductase activity following administration of a dec-2-ynol and dec-2-ynoic acid. Nagi, Marmoud N.; Suneja, Sanoj K.; Cook, Lynda; Cinti, Dominick L. (Health Cent., Univ. Connecticut, Farmington, CT 06030, USA). Arch. Biochem. Biophys., 293(1), 71-8 (English) 1992. CODEN: ABBIA4. ISSN: 0003-9861.There are some reagents with their cas registry numbers 4117-14-0 and 94497-70-8 are used in this study. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) The effects of administration of dec-2-ynol and dec-2-ynoic acid on the hepatic GSH content and hepatic microsomal trans-2-enoyl-CoA reductase activity were examd. in rat. Both compds., when administered i.p., caused a marked depletion of GSH levels and a corresponding inactivation of trans-2-enoyl-CoA reductase activity in both a time- and dose-dependent manner. The dec-2-ynoic acid caused greater hepatotoxicity than dec-2-ynol based on serum alanine transaminase activity. Based on the observations that (a) the alc. did not interact with GSH in the presence or absence of cytosol, (b) the spectral manifestation of the interaction between GSH and the alc. occurred only when NAD+ was added to the reaction mixt. contg. the cytosol and reactants, and (c) a similar absorbance spectrum was obtained following the interaction between aldehyde and GSH, it was concluded that dec-2-ynol is converted to an electrophile, dec-2-ynal, which causes depletion of GSH. The decrease in GSH content following administration of the acid appears to be due to activation of the acid to the electrophile, dec-2-ynoyl CoA, which then interacts with GSH, resulting in its depletion, based on the in vitro observations that (a) the acid did not interact with GSH in the presence or absence of cytosol, and (b) the spectral manifestation of interaction between GSH and dec-2-ynoyl CoA occurred both nonenzymically and enzymically in the presence of rat liver glutathione S-transferase. Bovine serum albumin stimulated the enzymic reaction. Comparable to the effects of GSH were the effects of dec-2-ynol, dec-2-ynal, dec-2-ynoic acid, and dec-2-ynoyl CoA on the microsomal trans-2-enoyl-CoA reductase activity in vitro. While the alc. had no effect on the enzyme activity, its electrophilic product, the aldehyde, was a potent inhibitor. Similarly, the acid did not inhibit the enzyme activity unless the acid was present at high concn.; however, its electrophilic product, the CoA thioester, was a very potent inhibitor at very low concn. .