Detection and possible origins of aminomalonic acid in protein hydrolysates
โ Scribed by Shelley D. Copley; Elizabeth Frank; Wolff M. Kirsch; Tad H. Koch
- Book ID
- 102988784
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 701 KB
- Volume
- 201
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
Aminomalonic acid (Ama) was first detected in alkaline hydrolysates of proteins in 1984. In this work we describe our search for the origin of aminomalonic acid in alkaline hydrolysates of proteins. We have developed a technique for quantitation of aminomalonic acid based upon gas chromatography/mass spectrometry. Using this technique, we find approximately 0.3 Ama/1000 amino acids in hydrolysates of Escherichia coli protein. We have demonstrated that Ama is not formed from any of the 20 major amino acids during the hydrolysis procedure. Furthermore, the amount of Ama found does not depend on the presence of small amounts of O2 during the hydrolysis. Thus far, we have not been able to demonstrate an artifactual origin for Ama. The results described above suggest that Ama may indeed be a constituent of proteins before the hydrolysis procedure. Possible origins of Ama include errors in protein synthesis and oxidative damage to amino acid residues in proteins.
๐ SIMILAR VOLUMES
Because of its unstable nature, glutamine is normally analyzed after being deamidated to the more stable glutamic acid. However, both glutamine and glutamic acid could be easily converted to pyroglutamic acid (5-oxoproline, 2-pyrrolidone-5carboxylic acid) in solution or in the dry state1-3. The form