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Journals / Gazi Üniversitesi Mühendislik Mimarlık Fakültesi Dergisi / 2014 / Cilt: 28 Sayı: 1

ISOLATION, INHIBITION AND KINETIC MODELLING OF ALKALINE PHOSPHATASE (ALP) ENZYME

Alkalen Fosfataz (Alp) Enziminin Özütlenmesi, İnhibisyonu Ve Kinetik Modellenmesi

Zahide Durak
Metin Gürü
Pages
209–215
Publication Date
2014-03-27
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

In this study, urea was found to cause noncompetetive inhibition and creatinine to cause uncompetetive inhibition on liver ALP.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:This study scopes the purification of alkaline phosphatase enzyme extracted from the liver and the investigation of kinetic properties for the reactions with and without inhibitor.
📊
Key Findings & Data:According to these values, substrate affinity (Km) and maximum velocity (Vmax) values were determined.
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Conclusion & Impact:In this study, urea was found to cause noncompetetive inhibition and creatinine to cause uncompetetive inhibition on liver ALP.
🔬Design:Araştırma Makalesi
📍Scope:Comprehensive Sample
⚙️Variables:Alkalen fosfataz · Michaelis Menten · yarışmasız inhibisyon

Abstract

This study scopes the purification of alkaline phosphatase enzyme extracted from the liver and the investigation of kinetic properties for the reactions with and without inhibitor. Michaelis Menten and Lineweaver Burk graphs were drawn by means of experimental results. Km and Vmax values were calculated from these graphics. According to these values, substrate affinity (Km) and maximum velocity (Vmax) values were determined. Values without inhibitor; Km= 0,047 Vmax=24,87; with urea inhibitor Km= 0,054 Vmax=20,83 ; with creatinin inhibitor Km= 0,037 Vmax=20,83. The experiments were repeated with inhibitory substance and inhibition type was established. How high blood urea and creatinine levels affected alkaline phosphatase activity were determined. In this study, urea was found to cause noncompetetive inhibition and creatinine to cause uncompetetive inhibition on liver ALP.

Özet

Bu çalışma, sıçan karaciğerinden özütlenen alkalen fosfataz (ALP) enziminin kısmen özütlenmesini, inhibitörsüz ve inhibitör varlığında kinetik özelliklerinin araştırılmasını kapsamaktadır. Deneysel sonuçlar yardımıyla Michaelis Menten ve Lineweaver Burk grafikleri çizildi. Bu grafiklerden Km ve Vmax değerleri hesaplandı. Değerler: İnhibitörsüz Km= 0,047 Vmax=24,87; Üre inhibitörlü Km= 0,054 Vmax=20,83 ; Kreatinin inhibitörlü Km= 0,037 Vmax=20,83 olarak hesaplanmıştır. Bu değerlere göre enzimin substrata ilgisi ve maksimum hız tespit edildi. İnhibitör maddeyle deneyler tekrarlandı ve inhibisyon tipi belirlendi. Kandaki yüksek üre ve kreatinin seviyesinin alkalen fosfataz enzimini nasıl etkilediği bulundu. Kandaki ALP (Alkalen Fosfataz) üzerinde ürenin inhibitör olarak kullanıldığı çalışmada reaksiyonun yarışmasız (nonkompetetif) bir reaksiyon, kreatininin inhibitör olarak kullanıldığı çalışmada ise reaksiyonun yarışmacı olmayan (unkompetetif) bir reaksiyonla gerçekleştiği tespit edilmiştir.

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Cite This Article

Durak, Z., Gürü, M. (2014). ISOLATION, INHIBITION AND KINETIC MODELLING OF ALKALINE PHOSPHATASE (ALP) ENZYME. Gazi Üniversitesi Mühendislik Mimarlık Fakültesi Dergisi, Cilt: 28 Sayı: 1, 209–215. https://ajindex.com/articles/1078353

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