Detail of "29836-26-8"

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Biological activity of preformed cholera toxin-ganglioside GM1 complex

Biological activity of preformed cholera toxin-ganglioside GM1 complex. Fiani, Maria Luisa; Macioce, P.; Gallina, A.; Tomasi, M. (Lab. Biol. Cell., Ist. Super. Sanita, Rome 00161, Italy). J. Neurosci. Res., 12(2-3), 325-34 (Russian) 1984. CODEN: JNREDK. ISSN: 0360-4012. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Synthetic and natural amphiphiles, octyl glucoside [29836-26-8], Nonidet P40 [9036-19-5], SDS [151-21-3], ganglioside GM1 [37758-47-7], and ganglioside GD1a [12707-58-3], interact with cholera toxin (CLT) and with its active region (promoter A). The formation of CLT-amphiphile complex leads to inhibition of ADP-ribosyltransferase [58319-92-9] activity, a characteristic of promoter A elicited after thiol reagents treatment. In all cases, the interaction produces the max. inhibitory effect above the crit. micellar concn. of amphiphiles, although monomers of SDS show inhibition activity as well. The gangliosides appear to be capable of altering the bilayer organization of membrane, similar to synthetic detergents. When CLT-ganglioside complexes were incubated with cell culture medium contg. 10% fetal calf serum (FCS), the ADP-ribosyltransferase activity was completely restored both in cholera toxin and in promoter A. Some protein of FCS, which is avid of gangliosides, seems to be responsible for the reversibility of inhibition. The active site of promoter A may be located in a hydrophobic pocket of the toxin structure. Furthermore, CLT was bound to reconstituted Sendai virus envelopes (RSVEs), contg. a small amt. of GM1. The RSVEs are made of membranous vesicles, capable of binding and fusing with host cell membrane. The incubation for 1 h of RSVE bearing CLT with Friend's erythroleukemic cells produced the stimulation of adenylate cyclase [9012-42-4]. This stimulation appears to be due to the translocation of the active subunit of CLT in the inner half of the plasma membrane.

Using substrate engineering to harness enzymatic promiscuity and expand biological catalysis

All Rights Reserved. Using substrate engineering to harness enzymatic promiscuity and expand biological catalysis. Lairson, Luke L.; Watts, Andrew G.; Wakarchuk, Warren W.; Withers, Stephen G.Some commonly used reagents like 10323-20-3 and 29836-26-8 are used in this experiment. (Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1, Can.). Nature Chemical Biology, 2(12), 724-728 (English) 2006 Nature Publishing Group. CODEN: NCBABT. ISSN: 1552-4450. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Despite their unparalleled catalytic prowess and environmental compatibility, enzymes have yet to see widespread application in synthetic chem. This lack of application and the resulting underuse of their enormous potential stems not only from a wariness about aq. biol. catalysis on the part of the typical synthetic chemist but also from limitations on enzyme applicability that arise from the high degree of substrate specificity possessed by most enzymes. This latter perceived limitation is being successfully challenged through rational protein engineering and directed evolution efforts to alter substrate specificity. However, such programs require considerable effort to establish. Here we report an alternative strategy for expanding the substrate specificity, and therefore the synthetic utility, of a given enzyme through a process of 'substrate engineering'. The attachment of a readily removable functional group to an alternative glycosyltransferase substrate induces a productive binding mode, facilitating rational control of substrate specificity and regioselectivity using wild-type enzymes. .