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Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal
ZusammenfassungIn Säurehydrolysaten verschiedener Laugenbackwaren (Brezeln, Knabberartikel) wurde eine im Aminosäurechromatogramm unmittelbar nach Pyridosin eluierende ninhydrinpositive Verbindung…
Type I reversible photochemistry of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore
Cyclic endoperoxides of beta-carotene, potential pro-oxidants, as products of chemical quenching of singlet oxygen.
On the reaction of glyoxal with proteins
Experiments with solutions containing Nα-acetylarginine and glyoxal showed that “Glarg” is formed quickly under physiological conditions, but is labile at higher temperatures as well as at low pH values.
1H NMR spectroscopic studies of the moenomycins
Highly resolved 1H NMR spectra of the moenomycin antibiotics can be obtained in D2O solution when the concentration is below the critical micelle concentration. The 600 MHz spectra are structurally…
1H NMR as a Tool for the Structure Elucidation of Moenomycin Antibiotics
It was found that the system moenomycin A–D2O–C6D6 after sonification yielded highly resolved 1H NMR spectra, probably due to the formation of a microemulsion.
Combined Approach of NMR and Molecular Dynamics within a biphasic Membrane Mimetic: Conformation and Orientation of the Bradykinin Antagonist Hoe 140
Structure of Rapamycin: An NMR and Molecular‐Dynamics Investigation
The highly active immunosuppressive antibiotic rapamycin is a specific inhibitor of a signal transduction pathway that results in exocytosis and transcription. We report the results of the homo- and…
Toward a mechanism for biliprotein lyases: revisiting nucleophilic addition to phycocyanobilin.
A generalized lyase reaction mechanism is proposed on the basis of the addition of thiol and imidazole to phycocyanobilin that can be transferred by the lyase to apoproteins by either back-isomerization or direct transfer, generating phyCoviolobilin-containing proteins.
Studies on the formation of lysinomethylalanine and histidinomethylalanine in milk products
- A. W. Walter, T. Henle, R. Haessner, H. Klostermeyer
- Chemistry, MedicineZeitschrift fur Lebensmittel-Untersuchung und…
- 1 September 1994
The formation of LMeAL as well as of HMeAL during food processing is negligible, and both compounds eluted clearly separated from other basic amino acids in the amino acid chromatogram.