Detail of "6090-95-5"

Reference

External yeast

External yeast .beta.Some chemicals with cas registry numbers like 9001-57-4 and 6090-95-5 are also used.-fructosidase. Affinity labeling of the active site. Braun, Hersz (Lab. Biochem., Eidg. Tech. Hochsch., Zurich, Switz.). Biochim. Biophys. Acta, 452(2), 452-7 (English) 1976. CODEN: BBACAQ. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Coduritol-B-epoxide, a compd. structurally related to the substrates of external yeast .beta.-fructosidase (EC 3.2.1.26), is an active-site directed inhibitor of this enzyme. The inactivation was irreversible and 1st order with respect to time and inhibitor concn. One mol. of inhibitor reacted with 1 mol. of the enzyme, causing inactivation. The inactivation was prevented by the presence of substrates. The pH dependence of inactivation showed 2 dissocg. groups in the enzyme with pKa values 3.05 and 6.8 being involved in the inactivation process. A carboxylate at the active site with pKa 3.05 may be the reactive group with conduritol-B-epoxide. .

Glucocerebrosidase deficiency and lysosomal storage of glucocerebroside induced in cultured macrophages

Glucocerebrosidase deficiency and lysosomal storage of glucocerebroside induced in cultured macrophages. Das, Pijush K.; Murray, Gary J.; Gal, Andrew E.; Barranger, John A. (Natl. Inst. Neurol. Commun. Disorders Stroke, NIH, Bethesda, MD 20892, USA). Exp. Cell Res., 168(2), 463-74 (English) 1987. CODEN: ECREAL. ISSN: 0014-4827. DOCUMENT TYPE: Journal CA Section: 14 (Mammalian Pathological Biochemistry) A cell culture model simulating the genetic deficiency of glucocerebrosidase has been developed, utilizing macrophages and conduritol B epoxide (CBE), the specific irreversible inhibitor of the enzyme. Rat peritoneal macrophage glucocerebrosidase was completely inhibited when cells were treated with 10 mM CBE for 16 h or 100 mM CBE for 2 h. The t1/2 of inactivation was 30 min at 10 mM concn. When cells were washed free of CBE, the enzyme activity reappeared linearly with time, reaching 50% of control activity 48 h after removal of the inhibitor. CBE-treated macrophages had normal phagocytic activity toward [3H]glycine-coupled latex beads and a normal no. of mannose receptors. CBE had no effect on other lysosomal enzymes.In this experiment, several chemicals are used like 6090-95-5 and 37228-64-1 When [14C]glucocerebroside, encapsulated in multilamellar liposomes with a-D-mannopyranoside covalently coupled to the surface, was fed to glucocerebrosidase-depleted macrophages, the radiolabeled glycolipid accumulated and was undegraded. Subcellular fractionation on a Percoll d. gradient demonstrated that the stored glucocerebroside in the CBE-treated macrophages was localized in lysosomes. .