Synthesis of alpha-fluorosulfonamides by electrophilic fluorination

Alpha-fluorosulfonamides were prepared by electrophilic fluorination of tertiary sulfonamides using N-fluorobenzenesulfonimide as fluorinating agent and utilizing the dimethoxybenzyl group (DMB) as a new sulfonamide protecting group. Removal of the DMB group with TFA/CH(2)Cl(2) gave primary and secondary alpha-fluorosulfonamides.     

Structural analysis of phosphatidylcholines by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

The utility of post-source decay (PSD) matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was investigated for the structural analysis of phosphatidylcholine (PC). PC did not produce detectable negative molecular ion from MALDI, but positive ions were observed as both [PC+H](+) and [PC+Na](+). The PSD spectra of the protonated PC species contained only one fragment corresponding to the head group (m/z 184), while the sodiated precursors produced many fragment ions, including those derived from the loss of fatty acids. The loss of fatty acid from the C-1 position (sn-1) of the glycerol backbone was favored over the loss of fatty acid from the C-2 position (sn-2). Ions emanating from the fragmentation of the head group (phosphocholine) included [PC+Na-59](+), [PC+Na-183](+) and [PC+Na-205](+), which corresponded to the loss of trimethylamine (TMA), non-sodiated choline phosphate and sodiated choline phosphate, respectively. Other fragments reflecting the structure of the head group were observed at m/z 183, 146 and 86. The difference in the fragmentation patterns for the PSD of [PC+Na](+) compared to [PC+H](+) is attributed to difference in the binding of Na(+) and H(+). While the proton binds to a negatively charged oxygen of the phosphate group, the sodium ion can be associated with several regions of the PC molecule. Hence, in the sodiated PC, intermolecular interaction of the negatively charged oxygen of the phosphate group, along with sodium association at multiple sites, can lead to a complex and characteristic ion fragmentation pattern. The preferential loss of sn-1 fatty acid group could be explained by the formation of an energetically favorable six-member ring intermediate, as apposed to the five-member ring intermediate formed prior to the loss of sn-2 fatty acid group.     

Gamow-Teller beta decay of the very neutron-deficientN=50 nuclide98Cd

For the first time, detailed decay-spectroscopic investigations were performed for the very neutron-deficientN=50 nuclide⁹⁸Cd. The⁹⁸Cd activity was produced in spallation reactions between 600 MeV protons and a natural tin target, yielding a⁹⁸Cd beam intensity of 10 to 60 atoms/s at the collector of the ISOLDE massseparator. By means of-ray and conversion-electron spectroscopy, 19 transitions were found to follow the ⁺/EC decay⁹⁸Cd⁹⁸Ag. The transitions at 61 and 107 keV were shown to beM1(+E2) andE2, respectively, and the⁹⁸Cd half-life was measured as 9.2±0.3 s. TheQ _EC value of⁹⁸Cd is determined semiempirically and is compared to model predictions together with the measuredQ _EC values of the neighbouring cadmium isotopes^100,102Cd and theN=50 isotones⁹²Mo,⁹⁴Ru, and⁹⁶Pd, taken from the literature. The newly established decay scheme of⁹⁸Cd includes 9 excited states of⁹⁸Ag. Four states at 1691, 1861, 2164, and 2544 keV are directly fed by 0⁺ 1⁺ Gamow-Teller beta transitions with a summed strength of 3.5 _–0.7 ^+0.8 . This value corresponds to 25±5% of the strength predicted for the GT transformation of a g_9/2 proton (in⁹⁸Cd) into a g_7/2 neutron (in⁹⁸Ag) by the extreme single-particle shell model. The GT-strength splitting and quenching, observed for⁹⁸Cd, are compared with the corresponding data for lighter even-even N=50 isotones, and are discussed with reference to the predictions of more sophisticated nuclear models. We find that only in some cases it is possible to explain qualitatively the observed GT strength distribution and its total magnitude without renormalizing the free-neutron value of the axial-vector coupling constant.Dedicated to Prof. P. Armbruster on the occasion of his 60th birthday     

Salmonella in foods: new enrichment procedure for TECRA Salmonella Visual Immunoassay using a single rv(R10) only, TT only, or dual rv(R10) and TT selective enrichment broths (AOAC official method 998.09): collaborative study

A collaborative study was conducted to compare a new enrichment procedure for the TECRA Salmonella Visual Immunoassay (TSVIA) with the reference method given in the U.S. Food and Drug Administration's Bacteriological Analytical Manual (7th Ed.). Three food types (milk powder, pepper, and soy flour) were analyzed in Australia and 3 food types (milk chocolate, dried egg, and raw turkey) were analyzed in the United States. Thirty-eight collaborators participated in the study. The TECRA method was evaluated using both Rappaport-Vassiliadis R10 (RV(R10)) and tetrathionate (TT) broths for selective enrichment. M broth cultures arising from each of the 2 selective enrichment broths were tested in the TSVIA using 2 individual wells, one for each selective broth, and a single well to test the pooled selective enrichment broths. The results for the pooled enrichment broths were reported elsewhere. This study presents the results for the use of single enrichment broths, i.e., RV(R10) only or TT only, with the TSVIA. No significant differences (p > 0.05) were observed for the pairwise comparison of the proportion of positive samples for either RV(R10) or TT used as a single enrichment broth for the TSVIA with that for the reference method.     

Mass spectrometric determination of selenenylsulfide linkages in rat selenoprotein P

The reversible formation of a selenenylsulfide linkage in mammalian thioredoxin reductase was identified as having a key role in its activity. Identification of selenenylsulfide and/or diselenide linkages is therefore critical to the determination of the structure and function of selenoproteins. A selenopeptide, (298)SGSAITUQCAENLPSLCSUQGLFAEEK(324) (U=selenocysteine), was isolated from a tryptic digest of rat selenoprotein P. Its two cysteine residues and two selenocysteine (Sec) residues were determined to be present in oxidized form by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The selenopeptide was subjected to partial reduction by dithiothreitol with immediate alkylation by iodoacetamide. This process was monitored by MALDI-TOFMS to determine the number of alkylations that had taken place. The partially reduced and alkylated peptides were then analyzed by nano-electrospray ionization tandem mass spectrometry and the results indicated that selenenylsulfide linkages Sec304-Cys314 and Cys306-Sec316 were present. It is concluded that selenoprotein P contains these two selenenylsulfide bonds.