Abstract
Analysis of the concentration of free amino acids in biological samples is useful in clinical diagnostics. However, currently available methods are time consuming, potentially delaying diagnosis. Therefore, the development of more rapid analytical tools is needed. In this study, a chemiluminescence detection method for amino acids was developed, and the conditions for the enzyme reaction and assay were examined. For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction. This method provided selective quantification from 1 to 20 μM for serine, proline, glycine, and leucine; 1 to 60 μM for asparagine; and 1 to 150 μM for histidine. This assay, which utilized aaRSs for the detection of amino acids, could be useful for simple and rapid analysis of amino acids in clinical diagnostics.
Similar content being viewed by others
References
Valerio, A., D’Antona, G., & Nisoli, E. (2011). Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evolutionary perspective. Aging, 3, 464–478.
Ohara, H., Ichikawa, S., Matsumoto, H., Akiyama, M., Fujimoto, N., Kobayashi, T., & Tajima, S. (2010). Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts. Journal of Dermatology, 37, 330–338.
Bannai, M., Kawai, N., Nagao, K., Nakano, S., Matsuzawa, D., & Shimizu, E. (2011). Oral administration of glycine increases extracellular serotonin but not dopamine in the prefrontal cortex of rats. Psychiatry and Clinical Neurosciences, 65, 142–149.
Yang, J.-H., Wada, A., Yoshida, K., Miyoshi, Y., Sayano, Y., Esaki, K., Kinoshita, M., Tomonaga, S., Azuma, N., Watanabe, M., Hamase, K., Zaitsu, K., Machida, T., Messing, A., Itohara, S., Hirabayashi, Y., & Furuya, S. (2010). Brain-specific Phgdh deletion reveals a pivotal role for L-serine biosynthesis in controlling the level of D-serine, an NMDA receptor co-agonist, in adult brain. Journal of Biological Chemistry, 285, 41380–41390.
Koning, T. J., Snell, K., Duran, M., Berger, R., Poll-The, B.-T., & Surtees, R. (2003). L-serine in disease and development. Biochemical Journal, 371, 653–661.
Lancha, A. H., Jr., Poortmans, J. R., & Pereira, L. O. (2009). The effect of 5 days of aspartate and asparagine supplementation on glucose transport activity in rat muscle. Cell Biochemistry and Function, 27, 552–557.
Yan, S. L., Wu, S. T., Yin, M. C., Chen, H. T., & Chen, H. C. (2009). Protective effects from carnosine and histidine on acetaminophen-induced liver injury. Journal of Food Science, 74, H259–H265.
Kugimiya, A., & Matsuzaki, E. (2014). Microfluidic analysis of serine levels using seryl-tRNA synthetase coupled with spectrophotometric detection. Applied Biochemistry and Biotechnology, 174, 2527–2536.
Kugimiya, A., & Takamitsu, E. (2013). Spectrophotometric detection of histidine and lysine using combined enzymatic reactions. Materials Science and Engineering C, 33, 4867–4870.
Kugimiya, A., Fukada, R., & Funamoto, D. (2013). A luminol chemiluminescence method for sensing histidine and lysine using enzyme reactions. Analytical Biochemistry, 443, 22–26.
Sekine, S., Nureki, O., Dubois, D. Y., Bernier, S., Chenevert, R., Lapointe, J., Vassylyev, D. G., & Yokoyama, S. (2003). ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. EMBO Journal, 22, 676–688.
Sekine, S., Shichiri, M., Bernier, S., Chênevert, R., Lapointe, J., & Yokoyama, S. (2006). Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Structure, 14, 1791–1799.
Ohtsuki, T., Watanabe, Y., Takemoto, C., Kawai, G., Ueda, T., Kita, K., Kojima, S., Kaziro, Y., Nyborg, J., & Watanabe, K. (2001). An “elongated” translation elongation factor Tu for truncated tRNAs in nematode mitochondria. Journal of Biological Chemistry, 276, 21571–21577.
Han, J. M., Jeong, S. J., Park, M. C., Kim, G., Kwon, N. H., Kim, H. K., Ha, S. H., Ryu, S. H., & Kim, S. (2012). Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell, 149, 410–424.
Brustein, V. P., Cavalcanti, C. L. B., Melo, M. R., Jr., Correia, M. T. S., Beltrão, E. I. C., & Carvalho, L. B., Jr. (2012). Chemiluminescent detection of carbohydrates in the tumoral breast diseases. Applied Biochemistry and Biotechnology, 166, 268–275.
Tan, H., & Song, Z. (2014). Human saliva-based quantitative monitoring of clarithromycin by flow injection chemiluminescence analysis: a pharmacokinetic study. Applied Biochemistry and Biotechnology, 172, 1320–1331.
Acknowledgments
This work was supported by the Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry (BRAIN).
Author information
Authors and Affiliations
Corresponding author
Electronic Supplementary Material
Below is the link to the electronic supplementary material.
Supplemental data 1
(PPTX 86 kb)
Rights and permissions
About this article
Cite this article
Kugimiya, A., Fukada, R. Chemiluminescence Detection of Serine, Proline, Glycine, Asparagine, Leucine, and Histidine by Using Corresponding Aminoacyl-tRNA Synthetases as Recognition Elements. Appl Biochem Biotechnol 176, 1195–1202 (2015). https://doi.org/10.1007/s12010-015-1639-6
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12010-015-1639-6