Detail of "11034-93-8"

Reference

Glycolipid-dependent agglutination of liposomes by Croton tiglium lectin

Glycolipid-dependent agglutination of liposomes by Croton tiglium lectin. Banerjee, Kalyan K.; Sen, A. (Dep. Chem., Bose Inst., Calcutta 700 009, India). FEBS Lett., 162(2), 248-51 (English) 1983. CODEN: FEBLAL. ISSN: 0014-5793.Several substances with their cas registry numbers 11034-93-8 and 60267-39-2 may be metioned in this study. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Croton tiglium Lectin (CTL), a protein with hemagglutinating and hemolytic activities which is specific for only complex carbohydrates, agglutinates phospholipid-glycolipid vesicles in the presence of 1 mM CaCl2. The CTL-induced agglutination of liposomes, which is not affected by phospholipid compn. and ionic strength, is completely inhibited by trypsin-released glycopeptides from sheep erythrocyte surface membranes, indicating that the phenomenon is mediated by lectin-carbohydrate interactions. Since the lectin-reactive glycolipids all carry the sequence Gal-Gal or their N-acetylated derivs. as the common structure denominator, it appears that the disaccharide unit Gal-Gal or their N-acetylated derivs. constitute an essential part of the carbohydrate hapten of the lectin. Lack of evidence for non-carbohydrate-dependent hydrophobic interaction of CTL with phospholipids and glycolipids lends support to the view that hemolysis is also a carbohydrate-dependent function of the lectin. .

D,L-a-Fluoropalmitic acid inhibits sphingosine base formation and accumulates in membrane lipids of cultured mammalian cells

D,L-a-Fluoropalmitic acid inhibits sphingosine base formation and accumulates in membrane lipids of cultured mammalian cells. Soltysiak, R. M.; Matsuura, F.; Bloomer, D.; Sweeley, C. C. (Dep. Biochem., Michigan State Univ.Chemicals with cas numbers 11034-93-8 and 89270-21-3 also play role., East Lansing, MI 48824, USA). Biochim. Biophys. Acta, 792(2), 214-26 (English) 1984. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) D,L-a-Fluoropalmitic acid (I) was synthesized by tosylation of methyl-D,L-a-hydroxypalmitate and displacement of the tosylated function by tetrabutylammonium fluoride in acetonitrile. Uptake and utilization of I by cultured Balb/c 3T3 cells were studied after presentation of the fluoro fatty acid analog complexed with bovine serum albumin. A concn. of 0.28 mM had very little effect on cell growth over several days of incubation, and cell morphol. was unchanged. Chromatog. and mass spectrometric analyses at 6 and 12 h of incubation showed that I was taken up by the cells and incorporated without modification as a fatty acyl moiety into select lipids. Significant levels of the compd. were found at 12 h in phosphatidylcholine (1.6%) and sphingomyelin (0.6%) fatty acids, but not in those of other phospholipids or neutral lipids. I represented a significant percentage of the fatty acids of neutral glycosphingolipids (1.4%) and ceramides (0.8%) by 12 h. The fluoro fatty acid was not incorporated into long-chain sphingolipid bases, and mass spectrometry failed to reveal addnl. C2 F-substituted compds. in cellular lipids. Cellular levels of triacylglycerols and phosphatidylcholine remained essentially unchanged or were slightly increased, whereas amts. of ceramide and gangliosides were decreased. Comparison of labeled palmitate incorporation into sphingolipid bases and fatty acids of sphingomyelin suggested inhibition of sphingosine synthesis by I. I inhibited the formation of palmitoyl-CoA by Balb/c 3T3 long-chain acyl-CoA synthetase in vitro. The results support involvement of CoA thiol ester-independent steps in modification of membrane lipids. .