Disease relevance of trifluoromethanesulfonic acid

• The structural relation of these components was investigated using deglycosylation with trifluoromethane-sulfonic acid, limited proteolysis with Staphylococcus aureus V8 protease, amino acid and carbohydrate composition analyses, sequence analysis, and monoclonal antibodies [1].
• Structural studies of the O-specific polysaccharide of Vibrio cholerae O8 using solvolysis with triflic acid [2].
• An acidic O-polysaccharide was obtained by mild acid degradation of the lipopolysaccharide of Escherichia coli O150 and studied by sugar and methylation analyses, triflic acid solvolysis, Smith degradation, (1)H and (13)C NMR spectroscopy, including 2D ROESY, (1)H,(13)C HSQC, HMQC-TOCSY, and HMBC experiments [3].
• The O-polysaccharide was obtained by mild acid degradation of the lipopolysaccharide of Providencia alcalifaciens O32 and studied by sugar and methylation analyses, solvolysis with triflic acid, (1)H and (13)C NMR spectroscopy, including two-dimensional (1)H,(1)H COSY, TOCSY, ROESY, H-detected (1)H,(13)C HSQC and HMBC experiments [4].

High impact information on trifluoromethanesulfonic acid

• The intact, fully glycosylated HSPG migrated as a broad smear (150-300 kD) by SDS-PAGE, but after deglycosylation with trifluoromethanesulfonic acid only a single approximately 40-kD band was seen [5].
• Chemical deglycosylation (apparently complete) of the C4 and Slp alpha chains with trifluoromethanesulfonic acid removes the molecular weight difference between them, suggesting that acquisition of extra glycosylation sites in the latter is responsible for this difference [6].
• Deglycosylation studies with trifluoromethanesulfonic acid pointed to the involvement of core mucin glycans in the A10 epitope [7].
• Ma552 reacted with H-CanAg, the MUC1 mucin purified from COLO 205, the binding increasing greatly upon partial deglycosylation of H-CanAg with trifluoromethanesulfonic acid [8].
• Chemical deglycosylation using trifluoromethanesulfonic acid yielded low molecular weight proteins, which could be analyzed for amino acid sequence, and also became susceptible to tryptic digestion [9].

Biological context of trifluoromethanesulfonic acid

• Trypsin treatment of trifluoromethanesulfonic acid-treated PSM releases the 81-residue tandem repeat as an ensemble of 81-residue glycopeptides with different glycosylation patterns [10].
• Acidic, nonbulky alcohols and triflic acid increase the rate of hydrogenation an order of magnitude above that which can be obtained with traditionally used methanol or water [11].
• Hydrolysis with trifluoromethanesulphonic acid yielded core proteins of 160 and 110 kDa (and minor bands of 90 and 60 kDa) [12].
• Synthesis of dixanthones and poly(dixanthone)s by cyclization of 2-aryloxybenzonitriles in trifluoromethanesulfonic acid [13].
• Hf(OTf)4 was the most active catalyst for this alkylation, and trifluoromethanesulfonic acid (triflic acid, TfOH) was also a good catalyst [14].

Anatomical context of trifluoromethanesulfonic acid

• If the canalicular bile salt-binding polypeptide was immunoprecipitated from Triton X-100-solubilized canalicular membranes and subsequently deglycosylated with trifluoromethanesulfonic acid, the apparent molecular weight was decreased from 100,000 to 48,000 (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) [15].
• Lactation-associated MUC1 was isolated from human milk and partially deglycosylated by trifluoromethanesulfonic acid to the level of core GalNAc residues [16].
• Deglycosylation of synaptic membranes (SMs) with endoglycosidase H, peptide:N-glycosidase F, trifluoromethane-sulfonic acid, and alkaline sodium borohydride indicated that GP50 is associated primarily, if not exclusively, with high-mannose and/or hybrid-type oligosaccharides and lacks complex N-linked and O-linked sugar chains [17].
• Treatment of the product from an avirulent strain of M. tuberculosis with trifluoromethanesulfonic acid released a single polypeptide with a molecular size of 23 kilodaltons, accounting for all of the insoluble cell wall protein [18].
• METHODS--Aggrecan was purified from human articular cartilage and deglycosylated with either bacterial glycosidases or trifluoromethanesulphonic acid (TFMS) [19].

Associations of trifluoromethanesulfonic acid with other chemical compounds

• This was achieved by Edman amino acid sequencing of the isolated tandem repeat after selective removal of non-C3-substituted, peptide-linked GalNAc residues by periodate oxidation and subsequent trimming of the remaining oligosaccharides to peptide-linked GalNAc residues by mild trifluoromethanesulfonic acid/anisole treatment [20].
• Chemical deglycosylation with trifluoromethanesulfonic acid, which cleaves O- and N-linked oligosaccharides except for the asparagine-linked N-acetylglucosamine, reduced the Mr of Fc gamma RIII to 21 to 36 kDa [21].
• Protonation of 3 with 2 equiv of triflic acid results in the protonation of both the PNP ligand and the metal hydride to form the dihydrogen complex [(H(2))Fe(PNHP)(dmpm)(CH(3)CN)](3+), 11 [22].
• Potato (Solanum tuberosum) lectin, which is a very highly glycosylated glycoprotein, has been completely deglycosylated by use of the trifluoromethanesulphonic acid reagent described by Edge, Faltnek, Hof, Reichert & Weber [(1981) Analyt. Biochem. 118, 131-137] [23].
• Determination of C-21 ketosteroids in serum using trifluoromethanesulfonic acid catalyzed precolumn dansylation and 1,1'-oxalyldiimidazole postcolumn peroxyoxalate chemiluminescence detection [24].

Gene context of trifluoromethanesulfonic acid

• MAb PANH3 raised against a synthetic peptide derived from the MG2 (MUC7) sequence reacted with the native molecule and stained a narrow smear of ca. 200,000 to 210,000 in Western blots of concentrated saliva and a lower-molecular-weight smear of trifluoromethanesulfonic-acid-treated MG2 [25].
• PANH2 binding was increased by deglycosylation with trifluoromethanesulfonic acid as well as with subsequent periodate treatment, and was eliminated by pronase treatment, strongly suggesting that MAb PANH2 was directed to a peptide epitope of MG1 [25].
• Assays for the detection of glycoconjugates (periodate oxidation, sialidase treatment, trifluoromethanesulfonic acid treatment) indicate that the hGH variant has carbohydrate moieties [26].
• Studies on the deglycosylation of porcine submaxillary mucin and human tracheobronchial mucin indicate that this approach provides more efficient removal of carbohydrate and less peptide core degradation than a more vigorous (25 degrees C) treatment with TFMSA alone [27].
• No binding occurred to the core protein of HSPG obtained after removal of HS with trifluoromethanesulfonic acid [28].

Analytical, diagnostic and therapeutic context of trifluoromethanesulfonic acid

• For the sequence analyses of the heavily glycosylated COOH-terminal portion, a chemical deglycosylation procedure with trifluoromethanesulfonic acid was employed [29].
• Bovine MAG was deglycosylated by trifluoromethanesulfonic acid, and binding of the M-proteins to MAG and to deglycosylated MAG was tested by immunoblotting [30].
• After treatment with trifluoromethanesulfonic acid, the molecular weight of the labeled protein decreased to 45,000, indicating that the receptor is glycosylated [31].
• Chemical treatments with trifluoromethanesulfonic acid and sodium metaperiodate destroyed the antigen determinants recognized by the above four mAbs, as detected by both ELISA and antibody absorption tests [32].
• When deglycosylated with trifluoromethanesulfonic acid, Ag-54 retained only 5% of its allergenic activity as compared to the native Ag-54 when tested by rocket immunoelectrophoresis and autoradiography [33].

References