Asparaginase from the hyperthermophilic microorganism Archaeoglobus fulgidus was cloned and expressed in Escherichia coli as a fusion protein with a polyhistidine tail. After heat treatment to denature most of the native E. coli proteins, the enzyme was purified by an
Journal of separation science, 32(13), 2305-2318 (2009-07-02)
The increase in our understanding of D-amino acid function and distribution in mammals is in many ways a result of the initial development of sensitive enantioselective separation strategies that allow for quantification in real biological samples. This article reviews progress
Journal of chromatography. A, 1218(40), 7130-7136 (2011-09-06)
D-Amino acids are increasingly being recognized as important signaling molecules in mammals, including humans. D-Serine and D-aspartate are believed to act as signaling molecules in the central nervous system. Interestingly, several other D-amino acids also occur in human plasma, but
A sensitive chiral capillary HPLC-MS/MS method well suited for the determination of amino acid enantiomers in biological samples was developed. The method involved precolumn derivatization of the sample with 7-fluoro-4-nitrobenzoxadiazole (NBD-F). After derivatization, NBD-amino acids were stacked on a C18
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