Detail of "12707-58-3"

Reference

Hormonal effects on the development changes of mouse small intestinal glycolipids

Hormonal effects on the development changes of mouse small intestinal glycolipids. Sato, Eiji; Fujie, Michio; Uezato, Tadayoshi; Fujita, Michiya; Nishimura, Kenji (Sch. Med., Hamamatsu Univ., Hamamatsu 431-31, Japan). Biochem. Biophys. Res. Commun., 119(3), 1168-73 (English) 1984. CODEN: BBRCA9. ISSN: 0006-291X. 53-06-5 and 71012-19-6 are also in the experiment. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Thyroxine [51-48-9] or cortisone [53-06-5] treatment of early postnatal mice accelerated normal developmental changes in the neutral glycosphingolipids and gangliosides of the small intestine. Gangliosides in the intestines of normal mice diminished after weaning, but hormone treatment resulted in precocious decreases in suckling mice. Of the major gangliosides present, the decrease was most prominent for ganglioside GD1a [12707-58-3]. In contrast, the neutral glycosphingolipid asialoganglioside GM1 [71012-19-6] increased after weaning, an effect that was induced in suckling mice by hormone treatment. Therefore, thyronine and(or) cortisone appear to be involved in the developmental changes in small intestine glycolipid compn. .

Interaction of cholera toxin with gangliosides: differential effects of the oligosaccharide of ganglioside GM1 and of micellar gangliosides

Interaction of cholera toxin with gangliosides: differential effects of the oligosaccharide of ganglioside GM1 and of micellar gangliosides. Tomasi, Maurizio; Battistini, Angela; Cardelli, Massimo; Sonnino, Sandro; D'Agnolo, Giuliano (Lab. Biol. Cell., Ist. Super. Sanita, Rome 00161, Italy). Biochemistry, 23(11), 2520-6 (English) 1984. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) UV difference absorption spectra of cholera toxin and its B protomer produced by the oligosaccharide moiety of GM1 [37758-47-7] were measured as a function of the oligosaccharide concn. In the presence of oligosaccharide, the spectrum was characterized by 3 peaks at 282, 288, and 292 nm. A linear increase in difference absorption was obsd. at this wavelengths vs. oligosaccharide concn.There are some reagents with their cas registry numbers 59247-13-1 and 37758-47-7 are used in this study.; a satn. effect occurred when the molar ratio of oligosaccharide to cholera toxin was >5. The features of the spectra indicated that the binding with the oligosaccharide affected the environment of tryptophan and tyrosine residues of protomer B. In good agreement with the above results, circular dichroic spectra indicated also a local effect of the binding, mostly restricted to protomer B; while the residues of protomer A remained largerly unperturbed. Difference absorption spectra were also measured for cholera toxin in the presence of ganglioside and detergent micelles. GD1a [12707-58-3] and GT1b [59247-13-1], were unable to bind cholera toxin and interacted with the protein by way of contaminating traces of GM1. The prepns. of GD1a and GT1b contained 0.8-1.0 and 0.4-0.5% (wt./wt.) of GM1, resp. The results obtained with GD1a and GT1b in contrast with the observations made with the oligosaccharide of GM1 indicated a major conformational change of the toxin structure. Thus, ganglioside micelle, behaving as a detergent, alters the structure of the toxin such as to induce the penetration of protomer A into the lipid milieu. In fact, isolated protomer A, incubated with ganglioside micelles, underwent a structural perturbation similar to that obsd. with the whole toxin. The complexes between gangliosides and cholera toxin or protomer A were also analyzed electrophoretically after digestion with thermolysin. After interaction with the gangliosides, protomer A was partially protected from the attack of the proteolytic enzyme in the isolated form and entire toxin. The specific redn. of the a-g disulfide bond of protomer A afforded complete protection in the intact toxin, but not in the isolated protomer A. Therefore, protomer A can enter the ganglioside micelles while the presence of protomer B accelerates this process after redn. of the a-g disulfide bond. Also, a possible role for protomer B in the lag period following the binding of the toxin to the membrane receptors, necessary for the insertion of protomer A into the membrane was suggested. .