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dc.contributor.authorYavuz Siliğ
dc.contributor.authorV. Kenan Çelik
dc.contributor.authorAtilla Atalay
dc.date.accessioned23.07.201910:49:13
dc.date.accessioned2019-07-23T16:20:21Z
dc.date.available23.07.201910:49:13
dc.date.available2019-07-23T16:20:21Z
dc.date.issued2000
dc.identifier.issn1300-0152
dc.identifier.urihttp://www.trdizin.gov.tr/publication/paper/detail/TWpZek1UTXo=
dc.identifier.urihttps://hdl.handle.net/20.500.12418/1209
dc.description.abstractBu çalışmada, $LD_10$(3 mg/ml) ve $LD_30$(9 mg/ml) dozlardında daminozid (süksinik asit, 2,2-dimetilhidrazid) uygulanmış Ross Pm-3 ırkı döletli tavuk yumurtalarından çıkarılan civcivlerin karaciğer mikrozomal Nitrozodimetilamin demetilaz (NDMAd) ve sitoplazmik Glutatyon-S-Transferaz (GST) aktiviteleri incelendi. NDMAd aktivitesi; Nitrozodimetilaminin (NDMA) demetilasyonu sonucu oluşan formaldehit'in Nash reaktifi ile tepkimesi sonucu meydana gelen sarı renkli bileşiğin (3,5-diasetil-1,4-dihidrolutidine) 412 nm de tayin edilmesiyle saptandı. Daminozidin $LD_30$ dozunun uygulandığı grupta, NDMAd aktivitisenide anlamlı bir artış (p>0.05) bulunmuşken $LD_10$ dozu uygulanan grupta NDMAd aktivitesinde belirgin bir artış (p>0.05) gözlenmemiştir. GST enzimi affinite kromatografisi ile saflaştırıldı ve GST aktivitesi glutatyon (GSH) ve 1-kloro-2,4-dinitrobenzen (CDNB) arasındaki tiyoester bağının oluşumu 340 nm de ölçülerek tayin edildi. Spesifik ve toplam GST aktiviteleri sırasıyla µmol/mg dk. ve ünite olarak verildi. $LD_10$ ve $LD_30$ dozlarında daminozid uygulanan grupların GST aktiviteleri kontrol grubuna kıyasla azalmış olarak bulundu (p<0.05). Sonuç olarak, $LD_30$ daminozid dozu NDMAd enzim aktivitesinin indüksiyonuna yolaçarken, $LD_10$ ve $LD_30$ dozlarının GST enzim aktivitesini inhibe ettiği gösterilmiştir. Enzim aktivitelerindeki bu değişiklikler detoksifikasyon işleminde yetersizliğe yolaçabilir.en_US
dc.description.abstractIn this study, microsomal nitrosodimethylamine demethylase (NDMAd) and cytoplasmic glutathione-s-tarnsferase (GST) activities in the livers of chicks obtained from the $LD_10$ (3 mg/ml) and $LD_130$ (9 mg/ml) doses of daminozide (Succinic acid 2,2-Dimethylhydrazide) injected Ross-Pm-3 fertilized chicken eggs were investigated. Spectrophotometric determination of NDMAd activity was performed at 412 nm by the detection of yellow coloured compound formed as a product of the reaction of formaldehyde with Nash reagent. No significant increase was observed in NDMAd activity (P&gt;0.05) of the group treated with $LD_10$ dose although NDMAd activity was found to be significantly increased (P&lt;0.05) in the gro up treated with $LD_30$ dose of daminozide. GST enzyem was purified by affinity chromatography and GST activity was determined by following the formation of thioester linkage between GSH and (1-Chloro-2,4-dinitrobenzene) CDNB at 340 nm. Specific and total GST activities were given as &micro;mol/mg min. and unite, respectively. GST activties of the groups treated with $LD_10$ and $LD_30$ doses of daminozide were found to be decreased (P&lt;0.05) when compared with those of the control group. In conclusion, $LD_30$ dose of daminozide led to the induction of NDMAd enzyme activity while $LD_10$ and $LD_130$ doses was shown to inhibit GST enzyme activity. The changes it these enzyme activities could lead to the insufficiency of the detoxification process.en_US
dc.language.isoturen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBiyolojien_US
dc.titleDaminozid uygulamasından sonra elde edilen civcivlerde karaciğer sitoplazmik glutatyon-S-Transferaz ve mikrozomal nitrozodimetilamin demetilaz aktivitelerindeki değişiklikleren_US
dc.title.alternativeChanges in liver cytoplasmic glutathione-S-tansferase and microsomal nitrosodimethylamine demethylase activities in chicks obtained following daminozide treatmenten_US
dc.typeotheren_US
dc.relation.journalTurkish Journal of Biologyen_US
dc.contributor.departmentSivas Cumhuriyet Üniversitesien_US
dc.identifier.volume24en_US
dc.identifier.issue1en_US
dc.identifier.endpage126en_US
dc.identifier.startpage119en_US
dc.relation.publicationcategoryDiğeren_US]


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