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dc.contributor.advisorAtalay, Atilla
dc.contributor.authorBakir, Sevtap
dc.date.accessioned2021-05-07T08:59:32Z
dc.date.available2021-05-07T08:59:32Z
dc.date.submitted1988
dc.date.issued2018-08-06
dc.identifier.urihttps://acikbilim.yok.gov.tr/handle/20.500.12812/601997
dc.description.abstractÖZET Bu çalışma, maya glukoz-6-fosfat dehidrogenaz'm ve tavşan kası piruvat kinazının N-Nitrozodietilamin ile inhibisyonunu, sığır serum albümini ve koenzimlerin koruyucu etkisini, N-Nitrozodietilamin'in her iki enzime bağlanma özelliklerini ve N-Nitrozodietilamin'in metabo lizmasının incelenmesini amaçlamıştır. Deney sırasında uygulanan inkübasyon koşullarında glukoz-6-fosfat dehidrogenaz'm % 50 'sini inhibe eden N-Nitrozodietilamin derişimi 4,5 mM, asetaldehid derişi mi ise 26 mM idi. İnkübasyon ortamına 13 ugm/ml. sığır serum albümini veya 0,1 mM NADP ilavesiyle N-Nitrozodie tilamin inhibisyonu % 50' ye düşmektedir. Ayrıca N-Nitro zodietilamin'in glukoz-6-fosfat dehidrogenaz'ı nonkompe- tatif olarak inhibe ettiği gözlenmiştir. Piruvat kinazın % 50 'sini inhibe eden N-Nitrozodietilamin derişimi 0,38 mM asetaldehit derişimiyse 36 mM bulunmuş tur. 33 ugm/ml sığır serum albümini veya 0,16 mM ADP ı katılmasıyla inhibisyon % 50' ye düşmektedir. Kinetik bulgular N-Nitrozodietilamin'in piruvat kinazı da non-56 kompetatif olarak inhibe ettiğini göstermiştir. N-Nitro- zodietilarain ile inkübasyondan sonra her iki enzimde diyaliz edilip, enzimlerle inhibitörün etkileşimi dalga boyuna karşı absorbans grafiği yoluyla araştırıldı. Yapılan poliakrilamit jel elektroforezi sonucu, N-Nitro- zodietilamin'in glukoz-6-fosfat dehidrogenaz ile bağlan dığı gözlendi. Bundan başka N-Nitrozodietilamin metabo lizması üzerinde deneysel çalışma uygulanıp, N-Nitrozo- dietilamin'den asetaldehit oluşma hızı hesaplandı.
dc.description.abstractSUMMARY THE IN VITRO INTERACTION BETWEEN N-NTTROSODIETHYLAMIN AND ITS STABLE METABOLITE ACETALDHYDE AND PYRUVATE KINASE AND GLUCOSE-6-PHOSPHATE DEHYDROGENASE ENZYMES The aim of this work is to investigate the inbiti- tion of the yeast glucose-6-phosphate dehydrogenase and rabbit muscle pyruvate kinase with N-Nitrosodiethy- lamin, the protective effect of bovine serum albumin and coenzymes, the binding properties of N-nitrosodi- ethylamine with both enzymes and the N-Nitrosodiethy- lamin metabolism. In the incubation conditions during the experi ments, the N-Nitrosodiethylamin concentration inhibits 50 % of glucose-6-phosphate dehydrogenase was 4.5 mM and that of acetaldehyde 26 mM. When 12 ugm/ml BSA or o,l mM NADP is added with the incubation medium, the N-Nitrosodiethylamin inhibition decrease by fifty percent. In addition, it has also been observed that N-Nitrosodiethylamin inhibits glucose-6-phosphate dehyd rogenase noncompetitively. The N-Nitrosodiethylamin concentration inhibits 5Ü % of pyruvate kinase was found to be 0.38 mM and that of acetaldehyde 36 mM. The inhibition decreased by 50 % when 22 ugra/ml bovine serum albumin or 0.L6 mM AIF was added. The kinetics5S findings also showed that N-Nitrosodiethylamin inhibits the pyruvate kinase noncompetitively. Both enzymes after incubation with N-Nitrosodiethylamin were dialyzed and the interaction of the enzymes with the inhibitor was investigated by absorbance graphy against the wavelenght. As a result polyacrylamide gel electropho resis carried out, it was observed that N-Nitrosodiethy lamin bound with glucose-6-phosphate dehydrogenase. Furthermore, experimental work on the N-Nitrosodiethyla min metabolism was carried out and the rate of acetal- dehyde formation from N-Nitrosodiethylamin has been calculated.en_US
dc.languageTurkish
dc.language.isotr
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightsAttribution 4.0 United Statestr_TR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectBiyokimyatr_TR
dc.subjectBiochemistryen_US
dc.titleN-nitrozodietilamin ve kararlı metaboliti olan asetaldehit`in piruvat kinaz ve glukoz -6-fosfat dehidiogenaz enzimleriyle in vitro etkileşimi
dc.title.alternativeThe In vitro interaction between N-nitrosodiethylamin and its stable metabolite acetaldhyde and pyruvate kinase and glucose -6-phosphate dehydrogenase enzymes
dc.typedoctoralThesis
dc.date.updated2018-08-06
dc.contributor.departmentBiyokimya Ana Bilim Dalı
dc.subject.ytmGlucosephosphate dehydrogenases
dc.subject.ytmAcetaldehyde
dc.subject.ytmDiethylnitrosamine
dc.subject.ytmPyruvate kinases
dc.identifier.yokid5028
dc.publisher.instituteSağlık Bilimleri Enstitüsü
dc.publisher.universityCUMHURİYET ÜNİVERSİTESİ
dc.identifier.thesisid5028
dc.description.pages75
dc.publisher.disciplineDiğer


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