Optimization of Storage and Stability of Camel Liver Glutathione S-Transferase

REFERENCES

• Atkinson, H.J.; Babbitt, P.C. Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold. Biochem. 2009, 48(46), 11108–16.
   PubMed Web of Science ®Google Scholar
• Jakoby, W.B. The Glutathione S-Transferases: A Group of Multifunctional Detoxification Proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 1978, 46, 383–414.
   PubMedGoogle Scholar
• Boyer, T.D. The Glutathione S-Transferases: An Update. Hepatol. 1989, 9(3), 486–496.
   PubMed Web of Science ®Google Scholar
• Mukanganyama, S.; Bezabih, M.; Robert, M.; Ngadjui, B.T.; Kapche, G.F.; Ngandeu, F.; Abegaz, B. The Evaluation Of Novel Natural Products as Inhibitors of Human Glutathione Transferase P1–1. J. Enzyme Inhib. Med. Chem. 2011, 26(4), 460–467.
   PubMed Web of Science ®Google Scholar
• Sheehan, D.; Meade, G.; Foley, V.M.; Dowd, C.A. Structure, Function and Evolution of Glutathione Transferases: Implications for Classification of Non-Mammalian Members of an Ancient Enzyme Superfamily. Biochem. J. 2001, 360(1), 1–16.
   PubMed Web of Science ®Google Scholar
• Dourado, D.F.; Fernandes, P.A.; Ramos, M.J. Mammalian Cytosolic Glutathione Transferases. Curr. Protein Peptide Sci. 2008, 9(4), 325–337.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D.; Flanagan, J.U.; Jowsey, I.R. Glutathione Transferases. Annu. Rev. Pharmacol. Toxicol. 2005, 45, 51–88.
   PubMed Web of Science ®Google Scholar
• Sun, H.D.; Ru, Y.W.; Zhang, D.J.; Yin, S.Y.; Yin, L.; Xie, Y.Y.; Guan, Y.F.; Liu, S.Q. Proteomic Analysis of Glutathione S-Transferase Isoforms in Mouse Liver Mitochondria, World J. Gastroenterol. 2012, 18(26), 3435–3442.
   PubMed Web of Science ®Google Scholar
• Awasthi, Y.C.; Sharma, R.; Singhal, S.S. Human Glutathione S-Transferases. Int. J. Biochem. 1994, 26(3), 295–308.
   PubMedGoogle Scholar
• Singhal, S.S.; Zimniak, P.; Sharma, R.; Srivastava, S.K.; Awasthi, S.; Awasthi, Y.C. A Novel Glutathione S-Transferase Isozyme Similar to GST 8–8 of Rat and mGSTA4–4 (GST 5.7) of Mouse Is Selectively Expressed in Human Tissues. Biochim Biophys. Acta 1994, 1204(2), 279–286.
   PubMed Web of Science ®Google Scholar
• Eaton, D.L.; Bammler, T.K. Concise Review of the Glutathione S-Transferases and Their Significance to Toxicology. Toxicol. Sci. 1999, 49(2), 156–164.
   PubMed Web of Science ®Google Scholar
• Gate, L.; Tew, K.D. Glutathione S-Transferases as Emerging Therapeutic Targets. Expert Opin. Ther. Targets 2001, 5(4), 477–489.
   PubMedGoogle Scholar
• Simic, T.; Savic-Radojevic, A.; Pljesa-Ercegovac, M.; Matic, M.; Mimic-Oka, J. Glutathione S-Transferases in Kidney and Urinary Bladder Tumors. Nat. Rev. Urol. 2009, 6(5), 281–289.
   PubMed Web of Science ®Google Scholar
• Thier, R.; Golka, K.; Bruning, T.; Ko, Y.; Bolt, H.M. Genetic Susceptibility to Environmental Toxicants: The Interface Between Human and Experimental Studies in the Development of New Toxicological Concepts. Toxicol. Lett. 2002, 127(1–3), 321–327.
   PubMed Web of Science ®Google Scholar
• Townsend, D.M.; Tew, K.D. The Role of Glutathione-S-Transferase in Anti-Cancer Drug Resistance. Oncogene. 2003, 22(47), 7369–7375.
   PubMed Web of Science ®Google Scholar
• Kaplowitz, N. Physiological Significance of Glutathione S-Transferases. Am. J. Physiol. 1980, 239(6), 439–444.
   Google Scholar
• Mosialou, E.; Morgenstern, R. Activity of Rat Liver Microsomal Glutathione Transferase Toward Products of Lipid Peroxidation and Studies of the Effect of Inhibitors on Glutathione-Dependent Protection Against Lipid Peroxidation. Arch. Biochem. Biophys. 1989, 275(1), 289–294.
   PubMed Web of Science ®Google Scholar
• Ishikawa, T. The ATP-Dependent Glutathione S-Conjugate Export Pump. Trends Biochem. Sci. 1992, 17(11), 463–468.
   PubMed Web of Science ®Google Scholar
• Keppler, D. Export Pumps for Glutathione S-Conjugates. Free Radic. Biol. Med. 1999, 27(9–10), 985–991.
   PubMed Web of Science ®Google Scholar
• Hinchman, C.A.; Ballatori, N. Glutathione Conjugation and Conversion to Mercapturic Acids Can Occur as an Intrahepatic Process. J. Toxicol. Environ. Health 1994, 41(4), 387–409.
   PubMed Web of Science ®Google Scholar
• Lee, T.K.; Li, L.; Ballatori, N. Hepatic Glutathione and Glutathione S-Conjugate Transport Mechanisms. Yale J. Biol. Med. 1997, 70(4), 287–300.
   PubMed Web of Science ®Google Scholar
• Rushmore, T.H.; Pickett, C.B. Glutathione S-Transferases, Structure, Regulation, and Therapeutic Implications. J. Biol. Chem. 1993, 268(16), 11475–11478.
   PubMed Web of Science ®Google Scholar
• Habig, W.H.; Pabst, M.J.; Fleischner, G.; Gatmaitan, Z.; Arias, I.M.; Jakoby, W.B. The Identity of Glutathione S-Transferase B With Ligandin, a Major Binding Protein of Liver. Proc. Natl. Acad. Sci. USA 1974, 71(10), 3879–3882.
   PubMed Web of Science ®Google Scholar
• Axarli, I.A.; Rigden, D.J.; Labrou, N.E. Characterization of the Ligandin Site of Maize Glutathione S-Transferase I. Biochem. J. 2004, 382(Pt 3), 885–893.
   PubMed Web of Science ®Google Scholar
• Park, J.S.; Han, K.Y.; Lee, J.H.; Song, J.A.; Ahn, K.Y.; Seo, H.S.; Sim, S.J.; Kim, S.W.; Lee, J. Solubility Enhancement of Aggregation-Prone Heterologous Proteins by Fusion Expression Using Stress-Responsive Escherichia coli Protein, RpoS. BMC Biotechnol. 2008, 8, 15.
   PubMed Web of Science ®Google Scholar
• Smith, D.B.; Johnson, K.S. Single-Step Purification of Polypeptides Expressed in Escherichia coli as Fusions With Glutathione S-Transferase. Gene 1988, 67(1), 31–40.
   PubMed Web of Science ®Google Scholar
• Guan, K.L.; Dixon, J.E. Eukaryotic Proteins Expressed in Escherichia coli: An Improved Thrombin Cleavage and Purification Procedure of Fusion Proteins With Glutathione S-Transferase. Anal. Biochem. 1991, 192(2), 262–267.
   PubMed Web of Science ®Google Scholar
• Vikis, H.G.; Guan, K.L. Glutathione-S-transferase-fusion Based Assays for Studying Protein-protein Interactions. Methods Mol. Biol. 2004, 261, 175–186.
   PubMedGoogle Scholar
• Zhan, B.; Liu, S.; Perally, S.; Xue, J.; Fujiwara, R.; Brophy, P.; Xiao, S.; Liu, Y.; Feng, J.; Williamson, A.; Wang, Y.; Bueno, L.L.; Mendez, S.; Goud, G.; Bethony, J.M.; Hawdon, J.M.; Loukas, A.; Jones, K.; Hotez, P.J. Biochemical Characterization and Vaccine Potential of a Heme-Binding Glutathione Transferase From the Adult Hookworm Ancylostoma caninum. Infect. Immun. 2005, 73(10), 6903–6911.
   PubMed Web of Science ®Google Scholar
• Zhan, B.; Perally, S.; Brophy, P.M.; Xue, J.; Goud, G.; Liu, S.; Deumic, V.; de Oliveira, L.M.; Bethony, J.; Bottazzi, M.E.; Jiang, D.; Gillespie, P.; Xiao, S.H.; Gupta, R.; Loukas, A.; Ranjit, N.; Lustigman, S.; Oksov, Y.; Hotez, P. Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases From the Human Hookworm Necator americanus. Infect. Immun. 2010, 78(4), 1552–1563.
   PubMed Web of Science ®Google Scholar
• Larsson, A.K.; Shokeer, A.; Mannervik, B. Molecular Evolution of Theta-Class Glutathione Transferase for Enhanced Activity With the Anticancer Drug 1,3-bis-(2-chloroethyl)-1-Nitrosourea and Other Alkylating Agents. Arch. Biochem. Biophys. 2010, 497(1–2), 28–34.
   PubMed Web of Science ®Google Scholar
• Lien, S.; Larsson, A.K.; Mannervik, B. The Polymorphic Human Glutathione Transferase T1–1, the Most Efficient Glutathione Transferase in the Denitrosation and Inactivation of the Anticancer Drug 1,3-bis(2-chloroethyl)-1-Nitrosourea. Biochem. Pharmacol. 2002, 63(2), 191–197.
   PubMed Web of Science ®Google Scholar
• Tripathi, T.; Na, B.K.; Sohn, W.M.; Becker, K.; Bhakuni, V. Structural, Functional and Unfolding Characteristics of Glutathione S-Transferase of Plasmodium vivax. Arch. Biochem. Biophys. 2009, 487, 115–22.
   PubMed Web of Science ®Google Scholar
• Ruzza, P.; Rosato, A.; Rossi, C.R.; Floreani, M.; Quintieri, L. Glutathione Transferases as Targets for Cancer Therapy. Anticancer Agents Med. Chem. 2009, 9(7), 763–777.
   PubMed Web of Science ®Google Scholar
• Kapoli, P.; Axarli, I.A.; Platis, D.; Fragoulaki, M.; Paine, M.; Hemingway, J.; Vontas, J.; Labrou, N.E. Engineering Sensitive Glutathione Transferase for the Detection of Xenobiotics. Biosens. Bioelectron. 2008, 24(3), 498–503.
   PubMed Web of Science ®Google Scholar
• Choi, J.W.; Kim, Y.K.; Song, S.Y.; Lee, I.H.; Lee, W.H. Optical Biosensor Consisting of Glutathione-S-Transferase for Detection of Captan. Biosens. Bioelectron. 2003, 18(12), 1461–1466.
   PubMed Web of Science ®Google Scholar
• Jemec, A.; Drobne, D.; Tisler, T.; Trebse, P.; Ros, M.; Sepcic, K. The Applicability of Acetylcholinesterase and Glutathione S-Transferase in Daphnia magna Toxicity Test. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2007, 144(4), 303–309.
   PubMed Web of Science ®Google Scholar
• Malik, A.; Al-Senaidy, A.; Skrzypczak-Jankun, E.; Jankun, J. A Study of the Anti-Diabetic Agents of Camel Milk. Int. J. Mol. Med. 2012, 30(3), 585–592.
   PubMed Web of Science ®Google Scholar
• Agrawal, R.P.; Jain, S.; Shah, S.; Chopra, A.; Agarwal, V. Effect of Camel Milk on Glycemic Control and Insulin Requirement in Patients With Type 1 Diabetes: 2-Years Randomized Controlled Trial. Eur. J. Clin. Nutr. 2011, 65(9), 1048–1052.
   PubMed Web of Science ®Google Scholar
• Maghraby, A.S.; Mohamed, M.A.; Abdel-Salam, A.M. Anti-Schistosomal Activity of Colostral and Mature Camel Milk on Schistosoma mansoni Infected Mice. Asia Pacific J. Clin. Nutr. 2005, 14(4), 432–438.
   PubMed Web of Science ®Google Scholar
• Liao, Y.; El-Fakkarany, E.; Lonnerdal, B.; Redwan, E.M. Inhibitory Effects of Native and Recombinant Full-Length Camel Lactoferrin and Its N and C Lobes on Hepatitis C Virus Infection of Huh7.5 Cells. J. Med. Microbiol. 2012, 61(Pt 3), 375–383.
   PubMed Web of Science ®Google Scholar
• el Redwan, R.M.; Tabll, A. Camel Lactoferrin Markedly Inhibits Hepatitis C Virus Genotype 4 Infection of Human Peripheral Blood Leukocytes. J. Immunoassay. Immunochem. 2007, 28(3), 267–277.
   PubMed Web of Science ®Google Scholar
• Al-Yousef, N.; Gaafar, A.; Al-Otaibi, B.; Al-Jammaz, I.; Al-Hussein, K.; Aboussekhra, A. Camel Urine Components Display Anti-Cancer Properties In Vitro. J. Ethnopharmacol. 2012, 143(3), 819–825.
   PubMed Web of Science ®Google Scholar
• Alhaidar, A.; Abdel Gader, A.G.; Mousa, S.A. The Antiplatelet Activity of Camel Urine. J. Altern. Complement. Med. 2011, 17(9), 803–808.
   PubMed Web of Science ®Google Scholar
• Hunaiti, A.A.; Sarhan, M.A. Purification and Characterization of Camel Liver Glutathione S-Transferase. Int. J. Biochem. 1987, 19(1), 71–77.
   PubMedGoogle Scholar
• Bradford, M.M. A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein–Dye Binding. Anal. Biochem. 1976, 72, 248–254.
   PubMed Web of Science ®Google Scholar
• Habig, W.H.; Pabst, M.J.; Jakoby, W.B. Glutathione S-Transferases. The First Enzymatic Step in Mercapturic Acid Formation. J. Biol. Chem. 1974, 249(22), 7130–7139.
   PubMed Web of Science ®Google Scholar
• Laemmli, U.K. Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4. Nature 1970, 227(5259), 680–685.
   PubMed Web of Science ®Google Scholar
• Raza, H.; Lakhani, M.S.; Ahmed, I.; John, A.; Morgenstern, R.; Montague, W. Tissue Specific Expression of Glutathione S-Transferases, Glutathione Content and Lipid Peroxidation in Camel Tissues. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1997, 118(4), 829–835.
   Web of Science ®Google Scholar
• Heljo, V.P.; Jouppila, K.; Hatanpaa, T.; Juppo, A.M. The Use of Disaccharides in Inhibiting Enzymatic Activity Loss and Secondary Structure Changes in Freeze-Dried Beta-Galactosidase During Storage. Pharm. Res. 2011, 28(3), 540–552.
   PubMed Web of Science ®Google Scholar
• Cray, C.; Rodriguez, M.; Zaias, J.; Altman, N.H. Effects of Storage Temperature and Time on Clinical Biochemical Parameters From Rat Serum. J. Am. Assoc. Lab. Anim. Sci. 2009, 48(2), 202–204.
   PubMed Web of Science ®Google Scholar
• Valeri, C.R.; Pivacek, L.E. Effects of the Temperature, the Duration of Frozen Storage, and the Freezing Container on In Vitro Measurements in Human Peripheral Blood Mononuclear Cells. Transfusion. 1996, 36(4), 303–308.
   PubMed Web of Science ®Google Scholar
• Vagenende, V.; Yap, M.G.; Trout, B.L. Mechanisms of Protein Stabilization and Prevention of Protein Aggregation by Glycerol. Biochem. 2009, 48(46), 11084–11096.
   PubMed Web of Science ®Google Scholar
• Yadav, J.K.; Prakash, V. Thermal Stability of Alpha-Amylase in Aqueous Cosolvent Systems. J. Biosci. 2009, 34(3), 377–387.
   PubMed Web of Science ®Google Scholar
• Gekko, K.; Timasheff, S.N. Thermodynamic and Kinetic Examination of Protein Stabilization by Glycerol. Biochemistry 1981, 20(16), 4677–4686.
   PubMed Web of Science ®Google Scholar
• Courtenay, E.S.; Capp, M.W.; Anderson, C.F.; Record, M.T. Jr. Vapor Pressure Osmometry Studies of Osmolyte–Protein Interactions: Implications for the Action of Osmoprotectants In Vivo and for the Interpretation of “Osmotic Stress” Experiments In Vitro. Biochem. 2000, 39(15), 4455–4471.
   PubMed Web of Science ®Google Scholar
• Timasheff, S.N. The Control of Protein Stability and Association by Weak Interactions With Water: How Do Solvents Affect These Processes? Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 67–97.
   PubMedGoogle Scholar
• Sinibaldi, R.; Ortore, M.G.; Spinozzi, F.; Carsughi, F.; Frielinghaus, H.; Cinelli, S.; Onori, G.; Mariani, P. Preferential Hydration of Lysozyme in Water/Glycerol Mixtures: A Small-Angle Neutron Scattering Study. J. Chem. Phys. 2007, 126(23), 235101.
   PubMed Web of Science ®Google Scholar
• Reddy, K.R.; Lilie, H.; Rudolph, R.; Lange, C. L-Arginine Increases the Solubility of Unfolded Species of Hen Egg White Lysozyme. Protein Sci. 2005, 14(4), 929–935.
   PubMed Web of Science ®Google Scholar
• Tischer, A.; Lilie, H.; Rudolph, R.; Lange, C. L-Arginine Hydrochloride Increases the Solubility of Folded and Unfolded Recombinant Plasminogen Activator rPA. Protein Sci. 2010, 19(9), 1783–1795.
   PubMed Web of Science ®Google Scholar
• Tsumoto, K.; Umetsu, M.; Kumagai, I.; Ejima, D.; Philo, J.S.; Arakawa, T. Role of Arginine in Protein Refolding, Solubilization, and Purification. Biotechnol. Prog. 2004, 20(5), 1301–1308.
   PubMed Web of Science ®Google Scholar
• Shiraki, K.; Kudou, M.; Fujiwara, S.; Imanaka, T.; Takagi, M. Biophysical Effect of Amino Acids on the Prevention of Protein Aggregation. J. Biochem. 2002, 132(4), 591–595.
   PubMed Web of Science ®Google Scholar
• Arakawa, T.; Tsumoto, K. The Effects of Arginine on Refolding of Aggregated Proteins: Not Facilitate Refolding, but Suppress Aggregation. Biochem. Biophys. Res. Commun. 2003, 304(1), 148–152.
   PubMed Web of Science ®Google Scholar
• Lin, T.Y.; Timasheff, S.N. On the Role of Surface Tension in the Stabilization of Globular Proteins. Protein Sci. 1996, 5(2), 372–381.
   PubMed Web of Science ®Google Scholar
• Taneja, S.; Ahmad, F. Increased Thermal Stability of Proteins in the Presence of Amino Acids. Biochem. J. 1994, 303(Pt 1), 147–153.
   PubMed Web of Science ®Google Scholar
• Akkemik, E.; Taser, P.; Bayindir, A.; Budak, H.; Ciftci, M. Purification and Characterization of Glutathione S-Transferase From Turkey Liver and Inhibition Effects of Some Metal Ions on Enzyme Activity. Environ. Toxicol. Pharmacol. 2012, 34(3), 888–94.
   PubMed Web of Science ®Google Scholar
• Frear, D.S.; Swanson, H.R. Biosynthesis of S-(4-ethylamino-6-isopropylamino-2-s-triazino) Glutathione: Partial Purification and Properties of a Glutathione S-Transferase From Corn. Phytochemistry 1970, 9(10), 2123–2132.
   Web of Science ®Google Scholar
• Guddewar, M.B.; Dauterman, W.C. Purification and Properties of a Glutathione-S-Transferase From Corn Which Conjugates s-Triazine Herbicides. Phytochemistry 1979, 18(5), 735–740.
   Web of Science ®Google Scholar
• Leavitt, J.R.C.; Penner, D. In Vitro Conjugation of Glutathione and Other Thiols With Acetanilide Herbicides and EPTC Sulfoxide and the Action of the Herbicide Antidote R-25788. J. Agric. Food Chem. 1979, 27(3), 533–536.
   Web of Science ®Google Scholar
• Guvercin, S.; Erat, M.; Sakiroglu, H. Determination of Some Kinetic and Characteristic Properties of Glutathione S-Transferase From Bovine Erythrocytes. Protein Pept. Lett. 2008, 15(1), 6–12.
   PubMed Web of Science ®Google Scholar