Detail of "3184-35-8"

Reference

Capillary gas chromatographic/mass spectrometric analysis of abnormal metabolites in hypoglycin-treated rat urine

Capillary gas chromatographic/mass spectrometric analysis of abnormal metabolites in hypoglycin-treated rat urine. Hine, David G.; Tanaka, Kay (Sch. Med., Yale Univ., New Haven, CT 06510, USA). Biomed. Mass Spectrom., 11(7), 332-9 (English) 1984. CODEN: BMSYAL. ISSN: 0306-042X. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Numerous abnormal metabolites were identified in large amts. in the urine of hypoglycin (I) [156-56-9]-treated rats using capillary gas chromatog./mass spectrometry-computer anal. These metabolites are not detectable in significant amts. in normal rats' urine. Ten were not previously assocd. with I administration: these were several hydroxy compds., including those from the valine and isoleucine pathways, 2-oxoadipic acid [3184-35-8], n-butyrylglycine [20208-73-5], and isovaleryl glucuronide [88070-93-3]. These results indicate that the pathways of isoleucine and valine metab. are inhibited at their resp. acyl-CoA dehydrogenation steps, as is the case for fatty acid, leucine, and lysine metab. The mass spectra of the trimethylsilyl derivs. of cis,cis-4,7-decadiene-1,10-dioic acid [38561-67-0], cis-4-decene-1,10-dioic acid [41221-65-2], cis-4-octene-1,8-dioic acid [38561-68-1], and (methylenecyclopropyl)acetylglycine [38561-70-5], which were previously identified using NMR and oxidative cleavage or acid hydrolysis, are presented for the 1st time.

Evidence for allosteric NADH regulation of Acinetobacter

Evidence for allosteric NADH regulation of Acinetobacter .alpha.-oxoglutarate dehydrogenase from multiple-inhibition studies. Hall, E.In this study， 9031-02-1 and 3184-35-8 are also used. Rachel; Weitzman, P. D. J. (Dep. Biochem., Univ. Leicester, Leicester, Engl.). Biochem. Biophys. Res. Commun., 74(4), 1613-17 (English) 1977. CODEN: BBRCA9. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Previous studies have suggested that the E1 component (.alpha.-oxoglutarate decarboxylase) of the oxoglutarate dehydrogenase complex of A. lwoffi is inhibited by the end-product, NADH. Multiple-inhibition studies in the simultaneous presence of NADH and .alpha.-oxoadipate, both competitive inhibitors with respect to .alpha.-oxoglutarate, indicate that NADH acts at an allosteric site within the multienzyme complex. .