Detail of "1182-42-9"

Reference

Effect of cholesteric liquid crystalline compounds on the radical polymerization of methyl methacrylate

Effect of cholesteric liquid crystalline compounds on the radical polymerization of methyl methacrylate. Deshpande, Dinkar D.; Aravindakshan, Perincheery (Dep. Chem.In this study， 61922-29-0 and 1182-42-9 are also used., Indian Inst. Technol., Bombay 400076, India). J. Macromol. Sci., Chem., A21(4), 523-31 (English) 1984. CODEN: JMCHBD. ISSN: 0022-233X. DOCUMENT TYPE: Journal CA Section: 35 (Chemistry of Synthetic High Polymers) Me methacrylate [80-62-6] was polymd. at 55° and at 65° using Bz2O2 as initiator in the presence of cholesterol (I) [57-88-5], 7 I derivs., N-(2-methoxybenzylidene)-p-butylaniline [89752-88-5] nematic liq. crystal, and rodlike mols., such as 2-butynediol [110-65-6] and diacetylene diol [55831-69-1]. The rates of polymn., activation energies, mol. wt., and tacticities of the polymers were discussed in light of monomer-additive interactions; monomer-additive complexes affected the polymn. rates. .

Purification of a soluble rat liver protein that stimulates microsomal 4-methyl sterol oxidase activity

Purification of a soluble rat liver protein that stimulates microsomal 4-methyl sterol oxidase activity. Gaylor, James L.; Delwiche, Constance V. (Div. Nutr. Sci., Cornell Univ., Ithaca, N. Y., USA). J. Biol. Chem., 251(21), 6638-45 (English) 1976. CODEN: JBCHA3. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) A soluble rat liver protein that stimulates microsomal methyl sterol oxidase activity was isolated and purified to homogeneity by salt fractionation, differential heat inactivation, 2 Ca-phosphate gel assocns., and Sephadex filtration. The protein may be dissocd. with detergent into subunits with a mol. wt. of .apprx.10,300, as detd. electrophoretically. Purified sol. protein enhances the obsd. rate of oxidative attack of the methyl sterol substrates, 4,4-dimethyl-5.alpha.-cholest-7-en-3.beta.-ol and 4.alpha.-methyl-5.alpha.-cholest-7-en-3.Several substances with their cas registry numbers 1510-20-9 and 1182-42-9 may be metioned in this study.beta.-ol. Addn. of increasing amts. of either partially purified or homogeneous sol. protein yielded hyperbolic stimulation, from which a K'm of .apprx.7 .mu.M was calcd. Sequential addns. of the sol. protein yielded equal increments of stimulation. These results are consistent with the suggestion that the sol. protein may be a reactant in the oxidative process. Methyl sterol oxidase is inhibited in vitro by cholesterol, several oxygenated sterols, and cholesterol esters. The extent of inhibition is much greater when the sol. protein is present in the incubation. The inhibition is competitive with respect to methyl sterol substrate; cholesterol succinate, a water-sol. ester, is strongly inhibitory, K'i(ester)/K'm(substrate) .apprx.0.2. Since end product inhibition of methyl sterol oxidase may be produced by accumulation of cholesterol or cholesterol metabolites, the sol. protein may participate in regulation of the activity of some microsomal enzymes of cholesterol biosynthesis. .