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D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri

Yıl 2020, , 1146 - 1153, 01.06.2020

İşıl Özyürek , Ramazan Kalın , Hasan Özdemir

https://doi.org/10.21597/jist.669441
Cited By: 3

Öz

Meme, tükürük ve diğer mukoza bezlerinden salgılanan laktoperoksidaz (LPO, E.C.1.11.1.7); antibakteriyel özelliğe sahip bir peroksidaz enzimidir. D-Penisilamin; Wilson hastalığı gibi birçok hastalığın tedavisinde kullanılan tiyol yan zincirine sahip bir amino asittir. Bu çalışmanın amacı, sığır laktoperoksidaz enzimine karşı D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin'in in vitro inhibisyon profillerini belirlemektir. LPO enzimi, % 62,25 verimle 357,92 kat afinite kromatografisi (Sepharose 4B-L-tirozin-sülfanamid) kullanılarak sığır sütünden saflaştırıldı. LPO; D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin tarafından etkili bir şekilde inhibe edildi. Bu moleküllerin IC50 değerleri sırasıyla 0,584, 0,207 ve 0,552 μM olarak bulundu. D-Penisilamin ve D-Penisilamin disülfit için yarışmalı inhibisyon gösterirken, N-Asetil-D-penisilamin için yarışmasız inhibisyon gösterdi.

Anahtar Kelimeler

Laktoperoksidaz penisilamin saflaştırma inhibisyon

Kaynakça

  • Bhushan R, Kumar R, 2009. Enantioresolution of DL-Penicillamine. Biomedical Chromatography, 24: 66-82.
  • Björck L, Claesson O, 1980. Correlation Between the Concentration of Hypothiocyanate and Antibacterial Effect of the Lactoperoxidase System Against Escherichia Coli. Journal of Dairy Science, 63: 919-922.
  • Bradford, MM, 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, 72(1-2): 248-251.
  • Budimir A, 2011. Metal İons, Alzheimer’s Disease and Chelation Therapy, Acta Pharmaceutıca, 61: 1-14.
  • Chipiso K, Duc T, Simoyi RH, 2019. Kinetics and Mechanism of Oxidation of N-Acetyl-D-Penicillamine in Acidified Iodate and Aqueous Iodine. South African Journal of Chemistry, 72: 1-9.
  • Colas C, Ku JM, Ortiz De Montellanao PR, 2002. Asp-225 And Glu-375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase. Journal of Biological Chemistry, 277: 7191-7200.
  • Gooneratne SR, Christensen DA, 1997. Effect of Chelating Agents on the Excretion of Copper, Zinc and İron in the Bile and Urine of Sheep. Veterinary Journal, 153: 171-178.
  • Jaffe IA, 1983. Penicillamine: An Anti-Rheumatoid Drug. American Journal of Medicine, 75: 63-68.
  • Kalın R, Atasever A, Özdemir H, 2014. The Single-Step Purification of Peroxidase by 4-Aminobenzohydrazide from Turkish Blackradish (Raphanus Sativus L.) and Turnip (Brassica Rapa L.) Roots. Food Chemistry, 150: 335-340.
  • Kark RAP, Poskanze DC, Bullock JB, Boylen G, 1971. Mercury Poisoning and its Treatment with N-Acetyl-D,L-Penicillamine, The New England Journal of Medicine, 285: 10-14.
  • Köksal Z, 2019. Inhibition Effects of Selected Thiophene-2-Sulfonamides on Lactoperoxidase. Drug and Chemical Toxicology, In Press. DOI: 10.1080/01480545.2019.1600532.
  • Köksal Z, Alım Z, Beydemir Ş, Özdemir H, (2016b). Potent Inhibitory Effects of Some Phenolic Acids on Lactoperoxidase. Journal of Biochemical and Molecular Toxicology, 30 (11): 533-538.
  • Köksal Z, Kalın R, Camadan Y, Usanmaz H, Almaz Z, Gülçin İ, Gökçen T, Gören AC, Özdemir H, 2017a. Secondary Sulfonamides as Effective Lactoperoxidase Inhibitors. Molecules: 22: 793-802.
  • Köksal Z, Kalın R, Gerni S, Gülçin İ, Özdemir H, 2017b. The Inhibition Effects of Some Natural Products on Lactoperoxidase Purified from Bovine Milk. Journal of Biochemical and Molecular Toxicology, 31 (9): E21939.
  • Köksal Z, Kalın R, Gülçin İ, Özdemir H, Atasever A, 2016a. The Impact of Some Avermectins on Lactoperoxidase in Bovine Milk. International Journal of Food Properties, 19 (6): 1207-1216.
  • Kussendrager KD, Van Hooijdonk ACM, 2000. Lactoperoxidase: Physico-Chemical Properties, Occurrence, Mechanism of Action and Applications. British Journal of Nutrition, 84 (1): 19-25.
  • Laemmli DK, 1970. Clevage of Structual Proteins During in Assembly of the Head of Bacteriophage T4. Nature, 227: 680-683.
  • Leroy EC, Trojanowska M, Smith EA, 1991. The Pathogenesis of Scleroderma (Systemic Sclerosis, Ssc). Clinical and Experimental Rheumatology, 9: 173-177.
  • Munro R, Capell HA, 1997. Disease-Modifying Drugs Series: Penicillamine. Brıtısh Journal of Rheumatology, 36 (1): 104-109.
  • Özdemir H, Aygül İ, Küfrevioğlu Öİ, 2001. Purification of Lactoperoxidase From Bovine Milk And İnvestigation of the Kinetic Properties. Preparative Biochemistry & Biotechnology, 31: 125-134.
  • Özdemir H, Uguz MT, 2005. In Vitro Effects of Some Anaesthetic Drugs on Lactoperoxidase Enzyme Activity. Journal of Enzyme Inhibition and Medicinal Chemistry, 20: 491-495.
  • Phelps DL, Lakatos L, Watts JL, 2001. Penicillamine for Preventing Retinopathy of Prematurity in Preterm İnfants. Cochrane Database of Systematic Reviews, 9: 1-26.
  • Reiter B, 1978. Review of the Progress of Dairy Science: Antimicrobial Systems in Milk. Journal of Dairy Research, 45: 131-147.
  • Sarikaya SBO, Şişecioğlu M, Çankaya M, Gülçin 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.
  • Seifu E, Buys EM, Donkin EF, 2005. Significance of the Lactoperoxidase System in The Dairy İndustry and its Potential Applications: A Review. Trends in Food Science & Technology, 16: 137-154.
  • Shindler JS, Bardsley W, 1975. Steady-State Kinetics of Lactoperoxidase With ABTS as Chromogens. Biochemical and Biophysical Research Communications, 67: 1307-1312.
  • Stephens AD, 1989. Cystinuria and İts Treatment: 25 Years Experience At St. Bartholomew’s Hospital. Journal of Inherited Metabolic Disease, 12: 197-209.
  • Şişecioğlu M, Çankaya M, Gülçin İ, Özdemir H, 2009b. The İnhibitory Effect of Propofol on Lactoperoxidase. Protein and Peptide Letters, 16: 46-49.
  • Şişecioğlu M, Çankaya M, Gülçin İ, Özdemir H, 2010a. Interactions of Melatonin and Serotonin to Lactoperoxidase Enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 25 (6): 7797-83.
  • Şişecioğlu M, Çankaya M, Özdemir H, 2009a. Effects of Some Vitamins on Lactoperoxidase Enzyme Activity. Internatıonal Journal for Vıtamın and Nutrıtıon Research, 79 (3): 188-194.
  • Şişecioğlu M, Gülçin İ, Çankaya M, Atasever A, Özdemir H, 2010b. The Effects of Norepinephrine on Lactoperoxidase Enzyme (LPO) . Scientific Research and Essays, 5 (11): 1351-1356.
  • Şişecioğlu M, Gülçin İ, Çankaya M, Özdemir H, 2012. The Inhıbıtory Effects of L-Adrenalıne on Lactoperoxıdase Enzyme Purıfıed from Bovıne Mılk. Internatıonal Journal of Food Propertıes, 15 (6): 1190-1199.
  • Şişecioğlu M, Uğuz MT, Çankaya M, Özdemir H, Gülçin İ, 2011. Effects of Ceftazidime Pentahydrate, Prednisolone, Amikacin Sulfate, Ceftriaxone Sodium and Teicoplanin on Bovine Milk Lactoperoxidase Activity. Internatıonal Journal of Pharmacology, 7: 79-83.
  • Walshe JM, 1956. Penicillamine, A New Oral Therapy for Wilson’s Disease. American Journal of Medicine, 21: 487-495.
  • Wolfson LM, Sumner SS, 1993. Antibacterial Activity of the Lactoperoxidase System: A Review. Journal of Food Protection, 56: 887-892.

The Inhibition Effects of D-Penicillamine, D-Penicillamine disulfide and N-Acetyl-D-Penicillamine on Lactoperoxidase Enzyme Activity

Yıl 2020, , 1146 - 1153, 01.06.2020

İşıl Özyürek , Ramazan Kalın , Hasan Özdemir

https://doi.org/10.21597/jist.669441
Cited By: 3

Öz

The lactoperoxidase (LPO, E.C.1.11.1.7) secreted from the breast, saliva and other mucous glands is a peroxidase enzyme with antibacterial properties. D-penicillamine is an amino acid with a thiol side chain, used in the treatment of many diseases such as Wilson disease. The aim of this study was to determine in vitro inhibition profiles of D-Penicillamine, D-Penicillamine disulfide and N-Acetyl-D-penicillamine against bovine lactoperoxidase enzyme. LPO enzyme was isolated from bovine milk using affinity chromatography (Sepharose 4B-L-tyrosine-sulphanamide) 357.92 fold with a yield of 62.25%. LPO was effectively inhibited by D-Penicillamine, N-Acetyl-D-penicillamine and D-Penicillamine disülfit. IC50 values of these molecules were found as 0.584, 0.207 and 0.552 𝜇M, respectively. D-Penicillamine, and D-Penicillamine disülfit exhibited competitive inhibition, and N-Acetyl-D-penicillamine showed noncompetitive inhibition.

Anahtar Kelimeler

Laktoperoksidaz penisilamin saflaştırma inhibisyon

Kaynakça

  • Bhushan R, Kumar R, 2009. Enantioresolution of DL-Penicillamine. Biomedical Chromatography, 24: 66-82.
  • Björck L, Claesson O, 1980. Correlation Between the Concentration of Hypothiocyanate and Antibacterial Effect of the Lactoperoxidase System Against Escherichia Coli. Journal of Dairy Science, 63: 919-922.
  • Bradford, MM, 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, 72(1-2): 248-251.
  • Budimir A, 2011. Metal İons, Alzheimer’s Disease and Chelation Therapy, Acta Pharmaceutıca, 61: 1-14.
  • Chipiso K, Duc T, Simoyi RH, 2019. Kinetics and Mechanism of Oxidation of N-Acetyl-D-Penicillamine in Acidified Iodate and Aqueous Iodine. South African Journal of Chemistry, 72: 1-9.
  • Colas C, Ku JM, Ortiz De Montellanao PR, 2002. Asp-225 And Glu-375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase. Journal of Biological Chemistry, 277: 7191-7200.
  • Gooneratne SR, Christensen DA, 1997. Effect of Chelating Agents on the Excretion of Copper, Zinc and İron in the Bile and Urine of Sheep. Veterinary Journal, 153: 171-178.
  • Jaffe IA, 1983. Penicillamine: An Anti-Rheumatoid Drug. American Journal of Medicine, 75: 63-68.
  • Kalın R, Atasever A, Özdemir H, 2014. The Single-Step Purification of Peroxidase by 4-Aminobenzohydrazide from Turkish Blackradish (Raphanus Sativus L.) and Turnip (Brassica Rapa L.) Roots. Food Chemistry, 150: 335-340.
  • Kark RAP, Poskanze DC, Bullock JB, Boylen G, 1971. Mercury Poisoning and its Treatment with N-Acetyl-D,L-Penicillamine, The New England Journal of Medicine, 285: 10-14.
  • Köksal Z, 2019. Inhibition Effects of Selected Thiophene-2-Sulfonamides on Lactoperoxidase. Drug and Chemical Toxicology, In Press. DOI: 10.1080/01480545.2019.1600532.
  • Köksal Z, Alım Z, Beydemir Ş, Özdemir H, (2016b). Potent Inhibitory Effects of Some Phenolic Acids on Lactoperoxidase. Journal of Biochemical and Molecular Toxicology, 30 (11): 533-538.
  • Köksal Z, Kalın R, Camadan Y, Usanmaz H, Almaz Z, Gülçin İ, Gökçen T, Gören AC, Özdemir H, 2017a. Secondary Sulfonamides as Effective Lactoperoxidase Inhibitors. Molecules: 22: 793-802.
  • Köksal Z, Kalın R, Gerni S, Gülçin İ, Özdemir H, 2017b. The Inhibition Effects of Some Natural Products on Lactoperoxidase Purified from Bovine Milk. Journal of Biochemical and Molecular Toxicology, 31 (9): E21939.
  • Köksal Z, Kalın R, Gülçin İ, Özdemir H, Atasever A, 2016a. The Impact of Some Avermectins on Lactoperoxidase in Bovine Milk. International Journal of Food Properties, 19 (6): 1207-1216.
  • Kussendrager KD, Van Hooijdonk ACM, 2000. Lactoperoxidase: Physico-Chemical Properties, Occurrence, Mechanism of Action and Applications. British Journal of Nutrition, 84 (1): 19-25.
  • Laemmli DK, 1970. Clevage of Structual Proteins During in Assembly of the Head of Bacteriophage T4. Nature, 227: 680-683.
  • Leroy EC, Trojanowska M, Smith EA, 1991. The Pathogenesis of Scleroderma (Systemic Sclerosis, Ssc). Clinical and Experimental Rheumatology, 9: 173-177.
  • Munro R, Capell HA, 1997. Disease-Modifying Drugs Series: Penicillamine. Brıtısh Journal of Rheumatology, 36 (1): 104-109.
  • Özdemir H, Aygül İ, Küfrevioğlu Öİ, 2001. Purification of Lactoperoxidase From Bovine Milk And İnvestigation of the Kinetic Properties. Preparative Biochemistry & Biotechnology, 31: 125-134.
  • Özdemir H, Uguz MT, 2005. In Vitro Effects of Some Anaesthetic Drugs on Lactoperoxidase Enzyme Activity. Journal of Enzyme Inhibition and Medicinal Chemistry, 20: 491-495.
  • Phelps DL, Lakatos L, Watts JL, 2001. Penicillamine for Preventing Retinopathy of Prematurity in Preterm İnfants. Cochrane Database of Systematic Reviews, 9: 1-26.
  • Reiter B, 1978. Review of the Progress of Dairy Science: Antimicrobial Systems in Milk. Journal of Dairy Research, 45: 131-147.
  • Sarikaya SBO, Şişecioğlu M, Çankaya M, Gülçin 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.
  • Seifu E, Buys EM, Donkin EF, 2005. Significance of the Lactoperoxidase System in The Dairy İndustry and its Potential Applications: A Review. Trends in Food Science & Technology, 16: 137-154.
  • Shindler JS, Bardsley W, 1975. Steady-State Kinetics of Lactoperoxidase With ABTS as Chromogens. Biochemical and Biophysical Research Communications, 67: 1307-1312.
  • Stephens AD, 1989. Cystinuria and İts Treatment: 25 Years Experience At St. Bartholomew’s Hospital. Journal of Inherited Metabolic Disease, 12: 197-209.
  • Şişecioğlu M, Çankaya M, Gülçin İ, Özdemir H, 2009b. The İnhibitory Effect of Propofol on Lactoperoxidase. Protein and Peptide Letters, 16: 46-49.
  • Şişecioğlu M, Çankaya M, Gülçin İ, Özdemir H, 2010a. Interactions of Melatonin and Serotonin to Lactoperoxidase Enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 25 (6): 7797-83.
  • Şişecioğlu M, Çankaya M, Özdemir H, 2009a. Effects of Some Vitamins on Lactoperoxidase Enzyme Activity. Internatıonal Journal for Vıtamın and Nutrıtıon Research, 79 (3): 188-194.
  • Şişecioğlu M, Gülçin İ, Çankaya M, Atasever A, Özdemir H, 2010b. The Effects of Norepinephrine on Lactoperoxidase Enzyme (LPO) . Scientific Research and Essays, 5 (11): 1351-1356.
  • Şişecioğlu M, Gülçin İ, Çankaya M, Özdemir H, 2012. The Inhıbıtory Effects of L-Adrenalıne on Lactoperoxıdase Enzyme Purıfıed from Bovıne Mılk. Internatıonal Journal of Food Propertıes, 15 (6): 1190-1199.
  • Şişecioğlu M, Uğuz MT, Çankaya M, Özdemir H, Gülçin İ, 2011. Effects of Ceftazidime Pentahydrate, Prednisolone, Amikacin Sulfate, Ceftriaxone Sodium and Teicoplanin on Bovine Milk Lactoperoxidase Activity. Internatıonal Journal of Pharmacology, 7: 79-83.
  • Walshe JM, 1956. Penicillamine, A New Oral Therapy for Wilson’s Disease. American Journal of Medicine, 21: 487-495.
  • Wolfson LM, Sumner SS, 1993. Antibacterial Activity of the Lactoperoxidase System: A Review. Journal of Food Protection, 56: 887-892.
Toplam 35 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Kimya Mühendisliği
Bölüm Kimya / Chemistry
Yazarlar

İşıl Özyürek 0000-0003-4896-5226

Ramazan Kalın 0000-0002-5917-1299

Hasan Özdemir 0000-0002-4059-0442

Yayımlanma Tarihi 1 Haziran 2020
Gönderilme Tarihi 2 Ocak 2020
Kabul Tarihi 1 Şubat 2020
Yayımlandığı Sayı Yıl 2020

Kaynak Göster

APA Özyürek, İ., Kalın, R., & Özdemir, H. (2020). D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri. Journal of the Institute of Science and Technology, 10(2), 1146-1153. https://doi.org/10.21597/jist.669441
AMA Özyürek İ, Kalın R, Özdemir H. D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri. Iğdır Üniv. Fen Bil Enst. Der. Haziran 2020;10(2):1146-1153. doi:10.21597/jist.669441
Chicago Özyürek, İşıl, Ramazan Kalın, ve Hasan Özdemir. “D-Penisilamin, D-Penisilamin disülfit Ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri”. Journal of the Institute of Science and Technology 10, sy. 2 (Haziran 2020): 1146-53. https://doi.org/10.21597/jist.669441.
EndNote Özyürek İ, Kalın R, Özdemir H (01 Haziran 2020) D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri. Journal of the Institute of Science and Technology 10 2 1146–1153.
IEEE İ. Özyürek, R. Kalın, ve H. Özdemir, “D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri”, Iğdır Üniv. Fen Bil Enst. Der., c. 10, sy. 2, ss. 1146–1153, 2020, doi: 10.21597/jist.669441.
ISNAD Özyürek, İşıl vd. “D-Penisilamin, D-Penisilamin disülfit Ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri”. Journal of the Institute of Science and Technology 10/2 (Haziran 2020), 1146-1153. https://doi.org/10.21597/jist.669441.
JAMA Özyürek İ, Kalın R, Özdemir H. D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri. Iğdır Üniv. Fen Bil Enst. Der. 2020;10:1146–1153.
MLA Özyürek, İşıl vd. “D-Penisilamin, D-Penisilamin disülfit Ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri”. Journal of the Institute of Science and Technology, c. 10, sy. 2, 2020, ss. 1146-53, doi:10.21597/jist.669441.
Vancouver Özyürek İ, Kalın R, Özdemir H. D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri. Iğdır Üniv. Fen Bil Enst. Der. 2020;10(2):1146-53.

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In Vitro Inhibition Effects of 2-Amino Thiazole Derivatives on Lactoperoxidase Enzyme Activity
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https://doi.org/10.17776/csj.1017247
Laktoperoksidaz Sistemine Karşı Sesamolün İnhibisyon Kinetiği
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Ramazan KALIN
https://doi.org/10.37989/gumussagbil.790529