Fragmentation studies of pentacoordinated bisaminoacylspirophosphoranes by negative electrospray ionization mass spectrometry.
Fragmentation pathways of a series of pentacoordinated bisaminoacylspirophosphoranes were elucidated by electrospray ionization multistage mass spectrometry (ESI-MS(n)) in negative mode. The deprotonated ions of pentacoordinated bisaminoacylspirophosphoranes tend to eliminate a corresponding amino acid to form base peak. The hydrogen/deuterium exchange experiment, the high-resolution mass spectrometry, (13)C stable isotope labeling experiment and theoretical calculations were used to rationalize the proposed fragmentation pathways and to verify the differences between the fragmentation pathways. The results indicate that the negative molecular ions of pentacoordinated bisaminoacylspirophosphoranes dissociate through its open-chain tricoordinated tautomers. The relative Gibbs free energies (ΔG) of the product ions and proposed fragmentation pathways were estimated using the B3LYP/6-31 + + G(d, p) model. The results have some potential applications in the identification structures of similar spirophosphorane compounds by ESI-MS(n).
The investigation of substituent effects on the fragmentation pathways of pentacoordinated phenoxyspirophosphoranes by ESI-MSn.
The fragmentation pathways of pentacoordinated phenoxyspirophosphoranes were investigated in the positive mode by electrospray ionization multistage mass spectrometry. The results demonstrate that the sodium adducts of the title compounds undergo two competitive fragmentation pathways, and the fragmentation patterns are heavily dependent on the various substituent patterns at the phenolic group. An electron-withdrawing substituent at the ortho-position always results in the removal of a corresponding phenol analogue, while cleavage by spiroring opening becomes the predominant fragmentation pathway if an electron-donating substituent is at the phenolic group. The substituent effects on the competitive fragmentation pathways were further elucidated by theoretical calculations, single crystal structure analysis, and high-resolution mass spectrometry. The results contribute to the understanding of the gas-phase fragmentation reactions and the structure identification of spirophosphorane analogues by electrospray ionization multistage mass spectrometry.
Comparative studies of α-Lactalbumin and lysozyme: Echidna lysozyme
Summaryα-Lactalbumin is a modifier protein for galactosyl transferase in the biosynthesis of lactose and lysozyme catalyses the cleavage of β(1–4) glycosidic linkages. It is now generally believed that α-lactalbumin and lysozyme have diverged from a common ancestor. Comparative studies of these proteins from several species are reported here.The presence of lactose and lactose synthetase activity is shown in mature milk samples from a variety of placental mammals (eutheria) and a pouch bearing mammal (marsupialia). The isolation of the α-lactalbumins involved and their properties are compared.The position is different in the milk samples of monotremes. The α-lactalbumin, lactose and lactose synthetase activity levels in the two platypus samples studied are very low. The levels of lactose and lactose synthetase activity in some echidna(Tachyglossus aculeatus) samples are low, but appreciable in others. No α-lactalbumin is present. The lysozyme activity is appreciable, some samples containing a different lysozyme from that present in others. One of these (designated echidna lysozyme I) is capable of lactose synthetase modifier activity in the presence of bovine “A protein”.The properties of this lysozyme are compared with those of lysozymes and α-lactalbumins from a variety of species and their significance is discussed.