New enzymatic method for l-arginine determination based on use of human arginase i and urease

Authors

  • Наталія Євгенівна Стасюк Institute of Cell Biology NAS of Ukraine 14/16 Drahomanov str., Lviv, Ukraine, 79005, Ukraine
  • Софія Ростиславівна Басс Ivan Franko National University of Lviv 4 Gryshevskoho str., Lviv, Ukraine, 79005, Ukraine
  • Галина Зуфарівна Гайда Institute of Cell Biology, NAS of Ukraine, 14/16 Drahomanov Str., Lviv, Ukraine, 79005, Ukraine
  • Хасмік Суренівна Єпрємян Scientific and Production Centre “Armbiotechnology” NAS of Armenia, 14 Guriyan str., Yerevan, Armenia, 0056, Armenia
  • Михайло Васильович Гончар Institute of Cell Biology NAS of Ukraine, 14/16 Drahomanov str., Lviv, Ukraine, 79005, Ukraine

DOI:

https://doi.org/10.15587/2313-8416.2015.45126

Keywords:

enzymatic assay, arginase I, urease, o-Phthalaldehyde, L-arginine, urea, ammonium, spectrophotometry

Abstract

It is developed a sensitive and selective method for quantitative analysis of L-arginine with spectrophotometric method of detection of the reaction product (ammonium) using o-Phthalaldehyde. The method is based on the use of highly purified arginase I and commercial urease. The new method is highly sensitive for L-arginine determination, a wide range of linearity and insensitivity to interfering influence of wide range of amino acids

Author Biographies

Наталія Євгенівна Стасюк, Institute of Cell Biology NAS of Ukraine 14/16 Drahomanov str., Lviv, Ukraine, 79005

Candidate of chemical sciences, Research Associate

Department of Analytical Biotechnology

Софія Ростиславівна Басс, Ivan Franko National University of Lviv 4 Gryshevskoho str., Lviv, Ukraine, 79005

Biological Faculty 

Галина Зуфарівна Гайда, Institute of Cell Biology, NAS of Ukraine, 14/16 Drahomanov Str., Lviv, Ukraine, 79005

Phylosophy doctor, chemistry, senior scientist

Department of analytical biotechnology, senior scientist

Хасмік Суренівна Єпрємян, Scientific and Production Centre “Armbiotechnology” NAS of Armenia, 14 Guriyan str., Yerevan, Armenia, 0056

Candidate of chemical sciences, Research Associate

Михайло Васильович Гончар, Institute of Cell Biology NAS of Ukraine, 14/16 Drahomanov str., Lviv, Ukraine, 79005

Doctor of Biological Sciences, Professor

Head of the Department

Department of Analytical Biotechnology

References

Yokoro, M., Suzuki, M., Murota, K., Otsuka, C., Yamashita, H., Takahashi, Y. et. al. (2012). Asymmetric Dimethylarginine, an Endogenous NOS Inhibitor, Is Actively Metabolized in Rat Erythrocytes. Bioscience, Biotechnology and Biochemistry, 76 (7), 1334–1342. doi: 10.1271/bbb.120086

Rotondo, R., Mastracci, L., Piazza, T., Barisione, G., Fabbi, M., Cassanello, M. et. al. (2008). Arginase 2 is expressed by human lung cancer, but it neither induces immune suppression, nor affects disease progression. International Journal of Cancer, 123 (5), 1108–1116. doi: 10.1002/ijc.23437

Lam, T.-L., Wong, G. K. Y., Chow, H.-Y., Chong, H.-C., Chow, T.-L., Kwok, S.-Y. et. al. (2010). Recombinant human arginase inhibits the in vitro and in vivo proliferation of human melanoma by inducing cell cycle arrest and apoptosis. Pigment Cell & Melanoma Research, 24 (2), 366–376. doi: 10.1111/j.1755-148x.2010.00798.x

Glazer, E. S., Stone, E. M., Zhu, C. et al. (2011). Bioengineered human arginase I with enhanced activity and stability controls hepatocellular and pancreatic carcinoma Transl. Oncol, 4 (3), 138–146.

Glazer, E. S., Stone, E. M., Zhu, C., Massey, K. L., Hamir, A. N., & Curley, S. A. (2011). Bioengineered Human Arginase I with Enhanced Activity and Stability Controls Hepatocellular and Pancreatic Carcinoma Xenografts. Translational Oncology, 4(3), 138–146. doi: 10.1593/tlo.10265

Morales, S. M. Cystinuria: diagnosis and therapeutic approach. (2011). An. Sist. Sanit. Navar, 34 (3), 453–461.

Lacroix, C., Caubet, C., Gonzalez-de-Peredo, A., Breuil, B., Bouyssié, D., Stella, A. et. al. (2014). Label-free Quantitative Urinary Proteomics Identifies the Arginase Pathway as a New Player in Congenital Obstructive Nephropathy. Molecular & Cellular Proteomics, 13 (12), 3421–3434. doi: 10.1074/mcp.m114.040121

Cohen, S. I. (1960). The determination of arginine released in human blood plasma after plasminogen activation. Use of a cation-exchange resin. Archives of Biochemistry and Biophysics, 86 (2), 166–168. doi: 10.1016/0003-9861(60)90397-0

Costin, J., Paul, F., Lewis, S. (2003). Selective determination of amino acids using flow injection analyses coupled with chemiluminescence detection, Anal. Chim. Acta., 408 (1), 67–77.

Fritz, J. H. (2013). Arginine Cools the Inflamed Gut. Infection and Immunity, 81 (10), 3500–3502. doi: 10.1128/iai.00789-13

Gayda, G. Z., Stasyuk, N. Ye., Gonchar, M. V. (2014). The methods of L-Arginine analysis (Review), Biotechnologia Acta, 7 (1). 31–39. doi: 10.15407/biotech7.01.031

Stasyuk, N.,Smutok, O., Gayda, G. et al. (2011). A new bi-enzyme potentiometric sensor for arginine analysis based on recombinant human arginase I and commercial urease. J. Mater. Sci. Eng. A., 1 (6), 819–827.

Stasyuk, N., Smutok, O., Gayda, G., Vus, B., Koval’chuk, Y., Gonchar, M. (2012). Bi-enzyme l-arginine-selective amperometric biosensor based on ammonium-sensing polyaniline-modified electrode. Biosensors and Bioelectronics, 37 (1), 46–52. doi: 10.1016/j.bios.2012.04.031

Stasyuk, N. E., Gaida, G. Z., Gonchar, M. V. (2013). L-arginine assay with the use of arginase I. Appl Biochem Microbiol, 49 (5), 529–534. doi: 10.1134/s000368381305013x

Mira de Orduña, R. (2001). Quantitative Determination of l -Arginine by Enzymatic End-Point Analysis. Journal of Agricultural and Food Chemistry, 49 (2), 549–552. doi: 10.1021/jf000522y

Gaede, G., Grieshaber, M. (1975). A rapid and specific enzymatic method for the estimation of l-arginine. Analytical Biochemistry, 66 (2), 393–399. doi: 10.1016/0003-2697(75)90606-5

Stasyuk, N., Gayda, G., Gayda, A. et al. (2011). The synthesis of affinity sorbents for purification of human arginase I from the recombinant yeast Hansenula polymorpha. Proc. Shevchenko Sci. Soc. Ser. Biochem, 28, 139–149.

Menshykov, V. V. (1987). The methods of laboratory investigations in clinical diagnostics. Мoscow: Мedicine, 215–219.

Kuo, M. T., Savaraj, N., Feun, L. G. (2010). Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes. Oncotarget, 1 (4), 246–251.

Goyal, S. S., Rains, D. W., Huffaker, R. C. (1988). Determination of ammonium ion by fluorometry or spectrophotometry after on-line derivatization with o-phthalaldehyde. Analytical Chemistry, 60 (2), 175–179. doi: 10.1021/ac00153a016

Ekanayake, S., Skog, K., Asp, N.-G. (2007). Canavanine content in sword beans (Canavalia gladiata): Analysis and effect of processing. Food and Chemical Toxicology, 45 (5), 797–803. doi: 10.1016/j.fct.2006.10.030

L-Arginine/Urea/Ammonia, UV method. Available at: https://www.nzytech.com/products-services/analytical-test-kits/ak00171/

Stasyuk, N. Ye., Gayda, G. Z., Gayda, A. V. et al. (2012). Enzymatic assay of L-arginine by the use of recombinant human arginase I. Ukrainica Biorganica Acta, 1, 31–37.

Published

2015-06-25

Issue

Section

Biological sciences