An in vitro experimental study on the interference of glyphosate on the urease enzyme

Kezban Kartlaşmış; Mehmet Tahir Hüsunet; Sevinç Püren Yücel Karakaya; Tuğba Polat; Zeynep Tan; Nurten Dikmen

Makale detayları

An in vitro experimental study on the interference of glyphosate on the urease enzyme

Yazarlar:

Kezban Kartlaşmış | Mehmet Tahir Hüsunet | Sevinç Püren Yücel Karakaya | Tuğba Polat | Zeynep Tan | Nurten Dikmen

Yayıncı:

Cukurova University

Ana Başlıklar:

Tıbbi Biyokimya - Amino Asitler ve Metabolitler

Dergi:

Cukurova Medical Journal Vol.49 Issue 3, pp.779-792

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001327871

pISSN:

2602-3032

Anahtar kelimeler:

Özet:

 Purpose: Exposure to glyphosate is increasing due to the density of agricultural areas in Türkiye. In this study, the possible interference effect of glyphosate on urease, an enzyme that is frequently used in the diagnosis and follow-up of many diseases and in the measurement of urea in biological samples was examined. Materials and Methods: First, glyphosate was observed to have a negative interference in experiments using solutions of varying concentrations of urea. Second, blood samples were examined using the urease-glutamate dehydrogenase GLDH and indirect nesslerization procedures to determine the effects of glyphosate on the results before and after its addition. To determine the morphological and chemical alterations, scanning electron microscope SEM and Fourier-transform infrared spectroscopy FTIR analyses were conducted, and binding patterns were established through molecular docking. Urea measurements conducted with urease-GLDH and indirect nesslerization demonstrated a negative interference on the results with glyphosate concentrations of 103, 104, and 105 M. Results: Morphological changes observed in the SEM analysis were supported by the 3228.25 O-H, 1642.08 CC, and 1531.20 N-O cm1 bonds formed in the FTIR analysis. Furthermore, the molecular docking analysis showed that glyphosate affected the urease via hydrogen bonding Gly13, Ser12, Lys14, Thr15, and Asp37 and hydrophobic interactions Val10, Asp37, and Glu98. It was hypothesized that these interacting amino acids limit the accessibility of the ureases active catalytic conformation andor impact the stability of the catalytic transition state. Conclusion: Glyphosate leads to negative interference in human serum urea assays, leading to incorrect test results in clinical biochemistry, microbiology, and agricultural laboratories. This effect should be considered when conducting analysis, and clinicians as well as hospital information management systems should be informed ahead of time, with special emphasis devoted to this interference.

 Purpose: Exposure to glyphosate is increasing due to the density of agricultural areas in Türkiye. In this study, the possible interference effect of glyphosate on urease, an enzyme that is frequently used in the diagnosis and follow-up of many diseases and in the measurement of urea in biological samples was examined. Materials and Methods: First, glyphosate was observed to have a negative interference in experiments using solutions of varying concentrations of urea. Second, blood samples were examined using the urease-glutamate dehydrogenase GLDH and indirect nesslerization procedures to determine the effects of glyphosate on the results before and after its addition. To determine the morphological and chemical alterations, scanning electron microscope SEM and Fourier-transform infrared spectroscopy FTIR analyses were conducted, and binding patterns were established through molecular docking. Urea measurements conducted with urease-GLDH and indirect nesslerization demonstrated a negative interference on the results with glyphosate concentrations of 103, 104, and 105 M. Results: Morphological changes observed in the SEM analysis were supported by the 3228.25 O-H, 1642.08 CC, and 1531.20 N-O cm1 bonds formed in the FTIR analysis. Furthermore, the molecular docking analysis showed that glyphosate affected the urease via hydrogen bonding Gly13, Ser12, Lys14, Thr15, and Asp37 and hydrophobic interactions Val10, Asp37, and Glu98. It was hypothesized that these interacting amino acids limit the accessibility of the ureases active catalytic conformation andor impact the stability of the catalytic transition state. Conclusion: Glyphosate leads to negative interference in human serum urea assays, leading to incorrect test results in clinical biochemistry, microbiology, and agricultural laboratories. This effect should be considered when conducting analysis, and clinicians as well as hospital information management systems should be informed ahead of time, with special emphasis devoted to this interference.

 Purpose: Exposure to glyphosate is increasing due to the density of agricultural areas in Türkiye. In this study, the possible interference effect of glyphosate on urease, an enzyme that is frequently used in the diagnosis and follow-up of many diseases and in the measurement of urea in biological samples was examined. Materials and Methods: First, glyphosate was observed to have a negative interference in experiments using solutions of varying concentrations of urea. Second, blood samples were examined using the urease-glutamate dehydrogenase GLDH and indirect nesslerization procedures to determine the effects of glyphosate on the results before and after its addition. To determine the morphological and chemical alterations, scanning electron microscope SEM and Fourier-transform infrared spectroscopy FTIR analyses were conducted, and binding patterns were established through molecular docking. Urea measurements conducted with urease-GLDH and indirect nesslerization demonstrated a negative interference on the results with glyphosate concentrations of 103, 104, and 105 M. Results: Morphological changes observed in the SEM analysis were supported by the 3228.25 O-H, 1642.08 CC, and 1531.20 N-O cm1 bonds formed in the FTIR analysis. Furthermore, the molecular docking analysis showed that glyphosate affected the urease via hydrogen bonding Gly13, Ser12, Lys14, Thr15, and Asp37 and hydrophobic interactions Val10, Asp37, and Glu98. It was hypothesized that these interacting amino acids limit the accessibility of the ureases active catalytic conformation andor impact the stability of the catalytic transition state. Conclusion: Glyphosate leads to negative interference in human serum urea assays, leading to incorrect test results in clinical biochemistry, microbiology, and agricultural laboratories. This effect should be considered when conducting analysis, and clinicians as well as hospital information management systems should be informed ahead of time, with special emphasis devoted to this interference.

 Amaç: Türkiyede tarım alanlarının yoğunluğu nedeniyle glifosata maruziyet artmaktadır. Bu çalışmada glifosatın birçok hastalığın tanı ve takibinde üre ölçümünde sıklıkla kullanılan bir enzim olan üreaz üzerindeki olası interferans etkisi incelendi. Gereç ve Yöntem: Ön denemelerde glifosatın, değişen konsantrasyonlarda üre solüsyonlarıyla negatif etkileşime sahip olduğu gözlendi. İn vitro ortamda glifosat eklenmesi öncesi ve sonrası sonuçlara etkisini belirlemek amacıyla kan örnekleri üreaz-GLDH ve dolaylı nesslerizasyon prosedürleri kullanılarak incelendi. Morfolojik ve kimyasal değişiklikler için taramalı elektron mikroskobu SEM ve Fouirer-Transform Infrared Spektrofotometre FTIR analizleri yapıldı ve moleküler kenetleme yoluyla bağlanma modelleri oluşturuldu. Üreaz-GLDH ve dolaylı nesslerizasyon ile gerçekleştirilen üre ölçümleri, 103, 104, ve 105 M konsantrasyonlarında glifosattaki sonuçlar üzerinde negatif bir etkileşim göstermiştir. Bulgular: SEM analizinde gözlenen morfolojik değişiklikler, FTIR analizinde oluşan 3228.25 O-H, 1642.08 CC, ve 1531.20 N-O cm1 bağları ile desteklenmiştir. Ayrıca moleküler kenetleme analizi, glifosatın, üreazı hidrojen bağı Gly13, Ser12, Lys14, Thr15, ve Asp37 ve hidrofobik etkileşimler Val10, Asp37, ve Glu98 yoluyla etkilediğini göstermektedir. Bu etkileşimli amino asitlerin, üreazın aktif katalitik konformasyonunun erişilebilirliğini sınırladığını veveya katalitik geçiş durumunun stabilitesini etkilediği öngörülmüştür. Sonuç: Glifosat, insan serum üre testlerinde negatif etkileşime yol açarak klinik biyokimya, mikrobiyoloji ve tarım laboratuvarlarında hatalı test sonuçlarına yol açar. Analiz yapılırken bu etki dikkate alınmalı ve klinisyenlerin yanı sıra hastane bilgi yönetim sistemleri de bu müdahaleye özel önem verilerek önceden bilgilendirilmelidir.

Makale detayları

An in vitro experimental study on the interference of glyphosate on the urease enzyme

Yazarlar:

Kezban Kartlaşmış | Mehmet Tahir Hüsunet | Sevinç Püren Yücel Karakaya | Tuğba Polat | Zeynep Tan | Nurten Dikmen

Yayıncı:

Cukurova University

Ana Başlıklar:

Tıbbi Biyokimya - Amino Asitler ve Metabolitler

Dergi:

Cukurova Medical Journal Vol.49 Issue 3, pp.779-792

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001327871

pISSN:

2602-3032

glyphosate

urease

interferenceGlifosat

girişim

üreaz

Sayı

Makale detayları

An in vitro experimental study on the interference of glyphosate on the urease enzyme

Yazarlar: Kezban Kartlaşmış | Mehmet Tahir Hüsunet | Sevinç Püren Yücel Karakaya | Tuğba Polat | Zeynep Tan | Nurten Dikmen

Yayıncı: Cukurova University

Ana Başlıklar: Tıbbi Biyokimya - Amino Asitler ve Metabolitler

Dergi: Cukurova Medical Journal Vol.49 Issue 3, pp.779-792

Belge Tipi: Makale

Yayın Tarihi: 9/2024

Belge Dili: İngilizce

Document ID (Org No.): 2001327871

pISSN: 2602-3032

glyphosate

urease

interferenceGlifosat

girişim

üreaz

Sayı

Yazarlar:

Kezban Kartlaşmış | Mehmet Tahir Hüsunet | Sevinç Püren Yücel Karakaya | Tuğba Polat | Zeynep Tan | Nurten Dikmen

Yayıncı:

Cukurova University

Ana Başlıklar:

Tıbbi Biyokimya - Amino Asitler ve Metabolitler

Dergi:

Cukurova Medical Journal Vol.49 Issue 3, pp.779-792

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001327871

pISSN:

2602-3032