References
- Akbaba, Y., Akıncıoğlu, A., Göçer, H., Göksu, S., Gülçin, I., & Supuran, C. T. (2014). Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins. Journal of Enzyme Inhibition and Medicinal Chemistry, 29(1), 35–42. https://doi.org/https://doi.org/10.3109/14756366.2012.750311
- Akbaba, Y., Bastem, E., Topal, F., Gülçin, I., Maraş, A., & Göksu, S. (2014). Synthesis and carbonic anhydrase inhibitory effects of novel sulfamides derived from 1-aminoindanes and anilines. Archiv Der Pharmazie, 347(12), 950–957. https://doi.org/https://doi.org/10.1002/ardp.201400257
- Akıncıoğlu, A., Akbaba, Y., Göçer, H., Göksu, S., Gülçin, İ., & Supuran, C. T. (2013). Novel sulfamides as potential carbonic anhydrase isoenzymes inhibitors. Bioorganic & Medicinal Chemistry, 21(6), 1379–1385. https://doi.org/https://doi.org/10.1016/j.bmc.2013.01.019
- Akıncıoğlu, A., Akıncıoğlu, H., Gülçin, İ., Durdagi, S., Supuran, C. T., & Göksu, S. (2015). Discovery of potent carbonic anhydrase and acetylcholine esterase inhibitors: Novel sulfamoylcarbamates and sulfamides derived from acetophenones. Bioorganic & Medicinal Chemistry, 23(13), 3592–3602. https://doi.org/https://doi.org/10.1016/j.bmc.2015.04.019
- Aksu, K., Nar, M., Tanc, M., Vullo, D., Gülçin, I., Göksu, S., Tümer, F., & Supuran, C. T. (2013). Synthesis and carbonic anhydrase inhibitory properties of sulfamides structurally related to dopamine. Bioorganic & Medicinal Chemistry, 21(11), 2925–2931. https://doi.org/https://doi.org/10.1016/j.bmc.2013.03.077
- Arabaci, B., Gulcin, I., & Alwasel, S. (2014). Capsaicin: A potent inhibitor of carbonic anhydrase isoenzymes. Molecules (Basel, Switzerland), 19(7), 10103–10114. https://doi.org/https://doi.org/10.3390/molecules190710103
- Artunc, T., Menzek, A., Taslimi, P., Gulcin, I., Kazaz, C., & Sahin, E. (2020). Synthesis and antioxidant activities of phenol derivatives from 1,6-bis(dimethoxyphenyl)hexane-1,6-dione. Bioorganic Chemistry, 100, 103884. https://doi.org/https://doi.org/10.1016/j.bioorg.2020.103884
- Asín-Prieto, E., Soraluce, A., Trocóniz, I. F., Campo Cimarras, E., Sáenz de Ugarte Sobrón, J., Rodríguez-Gascón, A., & Isla, A. (2015). Population pharmacokinetic models for cefuroxime and metronidazole used in combination as prophylactic agents in colorectal surgery: Model-based evaluation of standard dosing regimens. Int. J. Antimicrob. Agents, 45(5), 504–511. https://doi.org/https://doi.org/10.1016/j.ijantimicag.2015.01.008
- Atasever, A., Ozdemir, H., Gulcin, I., & Irfan Kufrevioglu, O. (2013). One-step purification of lactoperoxidase from bovine milk by affinity chromatography. Food Chemistry, 136(2), 864–870. https://doi.org/https://doi.org/10.1016/j.foodchem.2012.08.072
- Aydin, B., Gulcin, I., & Alwasel, S. H. (2015). Purification and characterization of polyphenol oxidase from Hemşin apple (Malus communis L.). International Journal of Food Properties., 18(12), 2735–2745. https://doi.org/https://doi.org/10.1080/10942912.2015.1012725
- Bayrak, C., Taslimi, P., Karaman, H. S., Gulcin, I., & Menzek, A. (2019). The first synthesis, carbonic anhydrase inhibition and anticholinergic activities of some bromophenol derivatives with S including natural products. Bioorganic Chemistry, 85, 128–139. https://doi.org/https://doi.org/10.1016/j.bioorg.2018.12.012
- Behçet, A., Çağlılar, T., Barut Celepci, D., Aktaş, A., Taslimi, P., Gök, Y., Aygün, M., Kaya, R., & Gülçin, İ. (2018). Synthesis, characterization and crystal structure of 2-(4-hydroxyphenyl)ethyl and 2-(4-nitrophenyl)ethyl substituted benzimidazolium bromide salts: Their inhibitory properties against carbonic anhydrase and acetylcholinesterase. Journal of Molecular Structure., 1170, 160–169. https://doi.org/https://doi.org/10.1016/j.molstruc.2018.05.077
- Beydemir, S., Ciftci, M., Küfrevioglu, O. I., & Büyükokuroglu, M. E. (2002). Effects of gentamicin sulfate on enzyme activities of carbonic anhydrase from human erythrocytes in vitro and from rat erythrocytes in vivo. Biological & Pharmaceutical Bulletin, 25(8), 966–969. https://doi.org/https://doi.org/10.1248/bpb.25.966
- Boots, J. W., & Floris, R. (2006). Lactoperoxidase: From catalytic mechanism to practical applications. International Dairy Journal., 16(11), 1272–1276. https://doi.org/https://doi.org/10.1016/j.idairyj.2006.06.019
- Bottoms, G. D., Fessler, J. F., Roesel, O. F., Moore, A. B., & Frauenfelder, H. C. (1981). Endotoxin-induced hemodynamic changes in ponies: Effects of Flunixin meglumine. American Journal of Veterinary Research, 42(9), 1514–1518.
- Boztaş, M., Çetinkaya, Y., Topal, M., Gülçin, İ., Menzek, A., Şahin, E., Tanc, M., & Supuran, C. T. (2015). Synthesis and carbonic anhydrase isoenzymes I, II, IX, and XII inhibitory effects of dimethoxybromophenol derivatives incorporating cyclopropane moieties. Journal of Medicinal Chemistry, 58(2), 640–650. https://doi.org/https://doi.org/10.1021/jm501573b
- Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–251. https://doi.org/https://doi.org/10.1016/0003-2697(76)90527-3
- Bursal, E., & Gulcin, I. (2011). Polyphenol contents and in vitro antioxidant activities of lyophilized aqueous extract of kiwifruit (Actinidia deliciosa). Food Research International., 44(5), 1482–1489. https://doi.org/https://doi.org/10.1016/j.foodres.2011.03.031
- Bursal, E., Köksal, E., Gülçin, İ., Bilsel, G., & Gören, A. C. (2013). Antioxidant activity and polyphenol content of cherry stem (Cerasus avium L.) determined by LC-MS/MS. Food Research International., 51(1), 66–74. https://doi.org/https://doi.org/10.1016/j.foodres.2012.11.022
- Caglayan, C., Taslimi, P., Türk, C., Kandemir, F. M., Demir, Y., & Gulcin, İ. (2019). Purification and characterization of the carbonic anhydrase enzyme from horse mackerel (Trachurus trachurus) muscle and the impact of some metal ions and pesticides on enzyme activity. Comparative Biochemistry and Physiology. Toxicology & Pharmacology : Cbp, 226, 108605https://doi.org/https://doi.org/10.1016/j.cbpc.2019.108605
- Cankaya, M., Sisecioglu, M., & Yoruk, O. (2006). In vitro effects of some antibiotic drugs on bovine lactoperoxidase enzyme. Turk J Med Sci, 36, 301–306.
- Cetin Cakmak, K., & Gülçin, I. (2019). Anticholinergic and antioxidant activities of usnic acid-An activity-structure insight. Toxicology Reports, 6, 1273–1280. https://doi.org/https://doi.org/10.1016/j.toxrep.2019.11.003
- Çetinkaya, Y., Göçer, H., Göksu, S., & Gülçin, İ. (2014). Synthesis and carbonic anhydrase isoenzymes I and II inhibitory effects of novel benzylamine derivatives. Journal of Enzyme Inhibition and Medicinal Chemistry, 29(2), 168–174. https://doi.org/https://doi.org/10.3109/14756366.2012.763163
- Çetinkaya, Y., Göçer, H., Gülçin, I., & Menzek, A. (2014). Synthesis and carbonic anhydrase isoenzymes inhibitory effects of brominated diphenylmethanone and its derivatives. Archiv Der Pharmazie, 347(5), 354–359. https://doi.org/https://doi.org/10.1002/ardp.201300349
- Chen, C., Li, J., Chen, P., Ding, R., Zhang, P., & Li, X. (2014). Occurrence of antibiotics and antibiotic resistances in soils from wastewater irrigation areas in Beijing and Tianjin, China. Environmental Pollution (Barking, Essex : 1987)), 193, 94–101. https://doi.org/https://doi.org/10.1016/j.envpol.2014.06.005
- Çoban, T. A., Beydemir, Ş., Gülçin, İ., & Ekinci, D. (2007). Morphine inhibits erythrocyte carbonic anhydrase in vitro and in vivo. Biological & Pharmaceutical Bulletin, 30(12), 2257–2261. https://doi.org/https://doi.org/10.1248/bpb.30.2257
- De Wit, J. N., & van Hooydonk, A. C. M. (1996). Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Netherlands Milk and Dairy Journal, 50, 227–244.
- Genc Bilgicli, H., Ergon, D., Taslimi, P., Tüzün, B., Akyazı Kuru, İ., Zengin, M., & Gülçin, İ. (2020). Novel propanolamine derivatives attached to 2-metoxifenol moiety: Synthesis, characterization, biological properties, and molecular docking studies. Bioorganic Chemistry, 101, 103969https://doi.org/https://doi.org/10.1016/j.bioorg.2020.103969
- Göçer, H., Akincioğlu, A., Göksu, S., Gülçin, İ., & Supuran, C. T. (2015). Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(2), 316–320. https://doi.org/https://doi.org/10.3109/14756366.2014.928704
- Göksu, S., Naderi, A., Akbaba, Y., Kalın, P., Akıncıoğlu, A., Gülçin, İ., Durdagi, S., & Salmas, R. E. (2014). Carbonic anhydrase inhibitory properties of novel benzylsulfamides using molecular modeling and experimental studies. Bioorganic Chemistry, 56, 75–82. https://doi.org/https://doi.org/10.1016/j.bioorg.2014.07.009
- Gülçin, I. (2006a). Antioxidant activity of caffeic acid (3,4-dihydroxycinnamic acid). Toxicology, 217(2-3), 213–220. https://doi.org/https://doi.org/10.1016/j.tox.2005.09.011
- Gülçin, I. (2006b). Antioxidant and antiradical activities of L-Carnitine. Life Sciences., 78(8), 803–811.
- Gülçin, I. (2007). Comparison of in vitro antioxidant and antiradical activities of L-tyrosine and L-Dopa. Amino Acids., 32, 431–438.
- Gülçin, I. (2008). Antioxidant and radical scavenging properties of curcumin. Chemico-Biological Interactions, 174, 27–37.
- Gülçin, I. (2009). Antioxidant activity of L-Adrenaline: An activity-structure insight. Chemico-Biological Interactions, 179(2-3), 71–80.
- Gülçin, I. (2010). Antioxidant properties of resveratrol: A structure-activity insight. Innovative Food Science & Emerging Technologies, 11, 210–218.
- Gülçin, I. (2012). Antioxidant activity of food constituents: An overview. Archives of Toxicology., 86(3), 345–391.
- Gülçin, I. (2020). Antioxidants and antioxidant methods: an updated overview. Archives of Toxicology, 94(3), 651–715. https://doi.org/https://doi.org/10.1007/s00204-020-02689-3
- Gülçin, İ., Scozzafava, A., Supuran, C. T., Akıncıoğlu, H., Koksal, Z., Turkan, F., & Alwasel, S. (2016). The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(6), 1095–1101. https://doi.org/https://doi.org/10.3109/14756366.2015.1094470
- Gülçin, I., Topal, F., Çakmakçı, R., Bilsel, M., Gören, A. C., & Erdogan, U. (2011). Pomological features, nutritional quality, polyphenol content analysis, and antioxidant properties of domesticated and 3 wild ecotype forms of raspberries (Rubus idaeus L.).). Journal of Food Science, 76(4), C585–C593. https://doi.org/https://doi.org/10.1111/j.1750-3841.2011.02142.x
- Gulçin, İ., Taslimi, P., Aygün, A., Sadeghian, N., Bastem, E., Kufrevioglu, O. I., Turkan, F., & Şen, F. (2018). Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes. International Journal of Biological Macromolecules, 119, 741–746. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2018.08.001
- Güllçin, I., Küfrevioğlu, O. I., & Oktay, M. (2005). Purification and characterization of polyphenol oxidase from nettle (Urtica dioica L.) and inhibitory effects of some chemicals on enzyme activity. Journal of Enzyme Inhibition and Medicinal Chemistry, 20(3), 297–302. https://doi.org/https://doi.org/10.1080/1475636032000141890
- Güney, M., Coşkun, A., Topal, F., Daştan, A., Gülçin, I., & Supuran, C. T. (2014). Oxidation of cyanobenzocycloheptatrienes: Synthesis, photooxygenation reaction and carbonic anhydrase isoenzymes inhibition properties of some new benzotropone derivatives. Bioorganic & Medicinal Chemistry, 22(13), 3537–3543. https://doi.org/https://doi.org/10.1016/j.bmc.2014.04.007
- Günsel, A., Bilgiçli, A. T., Barut, B., Taslimi, P., Özel, A., Gülçin, İ., Biyiklioglu, Z., & Yarasir, M. N. (2020). Synthesis of water soluble tetra-substituted phthalocyanines: Investigation of DNA cleavage, cytotoxic effects and metabolic enzyme inhibition. Journal of Molecular Structure., 1214, 128210. https://doi.org/https://doi.org/10.1016/j.molstruc.2020.128210
- Haddadin, M. S., Ibrahim, S. A., & Robinson, R. K. (1996). Preservation of raw milk by activation of the lactoperoxidase system. Food Control, 7(3), 149–152. https://doi.org/https://doi.org/10.1016/0956-7135(96)00023-0
- Innocenti, A., Beyza Öztürk Sarıkaya, S., Gülçin, İ., & Supuran, C. T. (2010). Carbonic anhydrase inhibitors. Inhibition of mammalian isoforms I-XIV with a series of natural product polyphenols and phenolic acids. Bioorganic & Medicinal Chemistry, 18(6), 2159–2164. https://doi.org/https://doi.org/10.1016/j.bmc.2010.01.076
- Innocenti, A., Gülçin, I., Scozzafava, A., & Supuran, C. T. (2010). Carbonic anhydrase inhibitors. Antioxidant polyphenols effectively inhibit mammalian isoforms I-XV. Bioorganic & Medicinal Chemistry Letters, 20(17), 5050–5053. https://doi.org/https://doi.org/10.1016/j.bmcl.2010.07.038
- Jacob, B. M., Essy, A. K., Sreekumar, B., & Haridas, M. (2000). Thiocyanate mediated antifungal and antibacterial property of goat milk. Life Sciences, 66(25), 2433–2439. https://doi.org/https://doi.org/10.1016/S0024-3205(00)80003-X
- Kalin, R., Koksal, Z., Kalin, P., Karaman, M., Gulcin, İ., & Ozdemir, H. (2020). In vitro effects of standard antioxidants on lactoperoxidase enzyme-A molecular docking approach. Journal of Biochemical and Molecular Toxicology, 34(1), e22421https://doi.org/https://doi.org/10.1002/jbt.22421
- Kaur, H., Singh, L., & Chibale, K. (2019). Structure elaboration of isoniazid: Synthesis, in silico molecular docking and antimycobacterial activity of isoniazid–pyrimidine conjugates. Molecular Diversity. https://doi.org/https://doi.org/10.1007/s11030-019-10004-1
- Kohler, H., & Jenzer, H. (1989). Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals. Free Radical Biology & Medicine, 6(3), 323–339. https://doi.org/https://doi.org/10.1016/0891-5849(89)90059-2
- Koksal, E., Bursal, E., Aggul, A. G., & Gulcin, I. (2012). Purification and characterization of peroxidase from sweet gourd (Cucurbita moschata Lam. Poiret). International Journal of Food Properties, 15(5), 1110–1119. https://doi.org/https://doi.org/10.1080/10942912.2010.513216
- Koksal, Z., Kalin, R., Kalin, P., Karaman, M., Gulcin, İ., & Ozdemir, H. (2020). Lactoperoxidase inhibition of some natural phenolic compounds: Kinetics and molecular docking studies. Journal of Food Biochemistry, 44(2), e13132https://doi.org/https://doi.org/10.1111/jfbc.13132
- Köksal, Z., Usanmaz, H., Bayrak, S., & Ozdemir, H. (2017). Improved chromatographic method for purification of lactoperoxidase from different milk sources. Preparative Biochemistry & Biotechnology, 47(2), 129–136. https://doi.org/https://doi.org/10.1080/10826068.2016.1185732
- Köksal, Z., Usanmaz, H., Özdemir, H., Gülçin, İ., & Güney, M. (2014). Inhibition effects of some phenolic and dimeric phenolic compounds on bovine lactoperoxidase (LPO) enzyme. International Journal of Academic Research, 6(2), 27–32. https://doi.org/https://doi.org/10.7813/2075-4124.2014/6-2/A.4
- Kose, L. P., Gülçin, İ., Özdemir, H., Atasever, A., Alwasel, S. H., & Supuran, C. T. (2016). The effects of some avermectins on bovine carbonic anhydrase enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(5), 773–778. https://doi.org/https://doi.org/10.3109/14756366.2015.1064406
- Kümmerer, K. (2009). Antibiotics in the aquatic environment-a review-Part I. Chemosphere, 75(4), 417–434. https://doi.org/https://doi.org/10.1016/j.chemosphere.2008.11.086
- Laemmli, D. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. https://doi.org/https://doi.org/10.1038/227680a0
- Lineweaver, H., & Burk, D. (1934). The determination of enzyme dissociation constants. Journal of the American Chemical Society, 56(3), 658–666. https://doi.org/https://doi.org/10.1021/ja01318a036
- Loftin, K. A., Henny, C., Adams, C. D., Surampali, R., & Mormile, M. R. (2005). Inhibition of microbial metabolism in anaerobic lagoons by selected sulfonamides, tetracyclines, lincomycin, and tylosin tartrate. Environmental Toxicology and Chemistry, 24(4), 782–788. https://doi.org/https://doi.org/10.1897/04-093r.1
- Nar, M., Çetinkaya, Y., Gülçin, İ., & Menzek, A. (2013). (3,4-Dihydroxyphenyl)(2,3,4-trihydroxyphenyl)methanone and its derivatives as carbonic anhydrase isoenzymes inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry, 28(2), 402–406. https://doi.org/https://doi.org/10.3109/14756366.2012.670807
- Owens, W. E., Ray, C. H., Watts, J. L., & Yancey, R. J. (1997). Antibiotic therapy success during lactation with antimicrobial susceptibility test results for bovine mastitis. Journal of Dairy Science., 80(2), 313–317. https://doi.org/https://doi.org/10.3168/jds.S0022-0302(97)75940-X
- Ozdemir, H., Aygul, I., & Kufrevioglu, O. I. (2001). Purification of lactoperoxidase from bovine milk and investigation of the kinetic properties. Preparative Biochemistry & Biotechnology, 31(2), 125–134. https://doi.org/https://doi.org/10.1081/PB-100103378
- Ozdemir, H., & Uğuz, M. T. (2005). In vitro effects of some anaesthetic drugs on lactoperoxidase enzyme activity. Journal of Enzyme Inhibition and Medicinal Chemistry, 20(5), 491–495. https://doi.org/https://doi.org/10.1080/14756360500225045
- Öztaşkın, N., Çetinkaya, Y., Taslimi, P., Göksu, S., & Gülçin, İ. (2015). Antioxidant and acetylcholinesterase inhibition properties of novel bromophenol derivatives. Bioorganic Chemistry, 60, 49–57. https://doi.org/https://doi.org/10.1016/j.bioorg.2015.04.006
- Oztürk Sarikaya, S. B., Topal, F., Sentürk, M., Gülçin, I., & Supuran, C. T. (2011). In vitro inhibition of α-carbonic anhydrase isozymes by some phenolic compounds. Bioorganic & Medicinal Chemistry Letters, 21(14), 4259–4262. https://doi.org/https://doi.org/10.1016/j.bmcl.2011.05.071
- Pan, M., & Chu, L. M. (2016). Adsorption and degradation of five selected antibiotics in agricultural soil. The Science of the Total Environment, 545-546, 48–56. https://doi.org/https://doi.org/10.1016/j.scitotenv.2015.12.040
- Pruitt, K. M., & Adamson, M. (1977). Enzyme activity of salivary lactoperoxidase adsorbed to human enamel. Infection and Immunity, 17(1), 112–116. https://doi.org/https://doi.org/10.1128/IAI.17.1.112-116.1977
- Reiter, B., & Härnulv, G. (1984). Lactoperoxidase antibacterial system: Natural occurrence, biological functions and practical applications. Journal of Food Protection, 47(9), 724–732. https://doi.org/https://doi.org/10.4315/0362-028X-47.9.724
- Sarikaya, S. B. O., Sisecioglu, M., Cankaya, M., Gulcin, İ., & Ozdemir, H. (2015). Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(3), 479–483. https://doi.org/https://doi.org/10.3109/14756366.2014.949254
- Schrödinger, L. (2017). Drug discovery suite.
- Sentürk, M., Gülçin, I., Beydemir, S., Küfrevioğlu, O. İ., & Supuran, C. T. (2011). In vitro inhibition of human carbonic anhydrase I and II isozymes with natural phenolic compounds. Chemical Biology & Drug Design, 77(6), 494–499. https://doi.org/https://doi.org/10.1111/j.1747-0285.2011.01104.x
- Sheikh, I. A., Jiffri, E. H., & Ashraf, G. M. (2018). Structural studies on inhibitory mechanisms of antibiotic, corticosteroid and catecholamine molecules on lactoperoxidase. Antican Res, 37, 6415–6420.
- Shindler, J. S., & Bardsley, W. G. (1975). Steady-state kinetics of lactoperoxidase with ABTS as chromogen. Biochemical and Biophysical Research Communications, 67(4), 1307–1312. https://doi.org/https://doi.org/10.1016/0006-291X(75)90169-2
- Sipe, H. J., Jordan, S. J., Hanna, P. M., & Mason, R. P. (1994). The metabolism of 17 beta-estradiol by lactoperoxidase: A possible source of oxidative stress in breast cancer. Carcinogenesis, 15(11), 2637–2643. https://doi.org/https://doi.org/10.1093/carcin/15.11.2637
- Şişecioğlu, M., Gulcin, I., & Cankaya, M. (2010). The effects of norepinephrine on lactoperoxidase enzyme (LPO). Scientific Research Essays, 5, 1351–1356.
- Şişecioğlu, M., Gulcin, I., & Çankaya, M. (2012). The inhibitory effects of L-Adrenaline on lactoperoxidase enzyme (LPO) purified from buffalo milk. International Journal of Food Properties., 15, 1182–1189.
- Şişecioğlu, M., Kirecci, E., & Cankaya, M. (2010). The prohibitive effect of lactoperoxidase system (LPS) on some pathogen fungi and bacteria. African Journal of Pharmacy and Pharmacology, 4, 671–677.
- Şişecioğlu, M., Cankaya, M., Gulcin, I., & Ozdemir, H. (2009). The Inhibitory effect of propofol on lactoperoxidase. Protein & Peptide Letters, 16(1), 46–49. https://doi.org/https://doi.org/10.2174/092986609787049394
- Şişecioğlu, M., Çankaya, M., Gülçin, İ., & Özdemir, H. (2010). Interactions of melatonin and serotonin with lactoperoxidase enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 25(6), 779–783. https://doi.org/https://doi.org/10.3109/14756360903425239
- Şişecioğlu, M., Uguz, M. T., Cankaya, M., Ozdemir, H., & Gulcin, I. (2011). Effects of ceftazidime pentahydrate, prednisolone, amikacin sulfate, ceftriaxone sodium and teicoplanin on bovine milk lactoperoxidase activity. International Journal of Pharmacology, 7(1), 79–83. https://doi.org/https://doi.org/10.3923/ijp.2011.79.83
- Small, P. M., & Chambers, H. F. (1990). Vancomycin for Staphylococcus aureus endocarditis in intravenous drug users. Antimicrobial Agents and Chemotherapy, 34(6), 1227–1231. https://doi.org/https://doi.org/10.1128/aac.34.6.1227
- Taslimi, P., & Gulcin, I. (2018). Antioxidant and anticholinergic properties of olivetol. Journal of Food Biochemistry, 42(3), e12516. https://doi.org/https://doi.org/10.1111/jfbc.12516
- Taslimi, P., Aslan, H. E., Demir, Y., Oztaskin, N., Maraş, A., Gulçin, İ., Beydemir, S., & Goksu, S. (2018). Diarylmethanon, bromophenol and diarylmethane compounds: Discovery of potent aldose reductase, α-amylase and α-glycosidase inhibitors as new therapeutic approach in diabetes and functional hyperglycemia. International Journal of Biological Macromolecules, 119, 857–863. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2018.08.004
- Taslimi, P., Gulcin, I., Ozgeris, B., Goksu, S., Tumer, F., Alwasel, S. H., & Supuran, C. T. (2016). The human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivatives. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(1), 152–157. https://doi.org/https://doi.org/10.3109/14756366.2015.1014476
- Topal, M., & Gulcin, I. (2014). Rosmarinic acid: A potent carbonic anhydrase isoenzymes inhibitor. Turkish Journal of Chemistry, 38, 894–902. https://doi.org/https://doi.org/10.3906/kim-1403-5
- Türkan, F., Huyut, Z., Taslimi, P., & Gülçin, İ. (2019). The effects of some antibiotics from cephalosporin groups on the acetylcholinesterase and butyrylcholinesterase enzymes activities in different tissues of rats. Archives of Physiology and Biochemistry., 125(1), 12–18. https://doi.org/https://doi.org/10.1080/13813455.2018.1427766
- Türkan, F., Huyut, Z., Taslimi, P., Huyut, M. T., & Gülçin, İ. (2020). Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different rat tissues in vivo for drug development research. Drug and Chemical Toxicology., 43(4), 423–428. https://doi.org/https://doi.org/10.1080/01480545.2018.1497644
- White, W. E., Pruitt, K. M., & Mansson-Rahemtulla, B. (1983). Peroxidase-thiocyanate-peroxide antibacterial system does not damage DNA. Antimicrobial Agents and Chemotherapy, 23(2), 267–272. https://doi.org/https://doi.org/10.1128/aac.23.2.267
- Wolfson, L. M., & Sumner, S. S. (1993). Antibacterial Activity of the Lactoperoxidase System: A Review. Journal of Food Protection, 56(10), 887–892. https://doi.org/https://doi.org/10.4315/0362-028X-56.10.887
- Yan, C., Yang, Y., Zhou, J., Liu, M., Nie, M., Shi, H., & Gu, L. (2013). Antibiotics in the surface water of the Yangtze Estuary: Occurrence, distribution and risk assessment. Environmental Pollution (Barking, Essex : 1987)), 175, 22–29. https://doi.org/https://doi.org/10.1016/j.envpol.2012.12.008
- Yıldırım, A., Atmaca, U., Keskin, A., Topal, M., Çelik, M., Gülçin, İ., & Supuran, C. T. (2015). N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes I and II. Bioorganic & Medicinal Chemistry, 23(10), 2598–2605. https://doi.org/https://doi.org/10.1016/j.bmc.2014.12.054
- Zhang, R., Zhang, G., Zheng, Q., Tang, J., Chen, Y., Xu, W., Zou, Y., & Chen, X. (2012). Occurrence and risks of antibiotics in the Laizhou bay, China: Impacts of river discharge. Ecotoxicology and Environmental Safety, 80, 208–221. https://doi.org/https://doi.org/10.1016/j.ecoenv.2012.03.002