İnsan Eritrosit Aldehit Dehidrogenazının Kısmen Saflaştırılarak Kinetik Özelliklerinin İncelenmesi

Year 1988, Volume: 41 Issue: 2, 211 - 222, 30.06.1988

Zuhal Yurtaslan

Abstract

İnsan eritrosit aldehit dehidrogenazı kısmen saflaştırılarak kinetik özellikleri incelendi. Enzimin kullanılan substratlarla MichaelisMenten kinetiğine uygun davrandığı tespit edildi. 10 4M disülfiram ile enzim aktivitesinde yaklaşık © 50 inhibisyon meydana geldi. 1 mM 8-merkaptoetanol ilavesi ile bu intibisyon tamamen ortadan kalktığı halde redüklenmiş glutatyonun etkisi olmadı. 1,5 mM Mg” ve Car un enzim aktivitesinde sırasıyla 96 45,16 ve 9 54,84 aktivitasyona yol açtığı görüldü. 1,5 mM Hgt'ise yaklaşık X 90,32inhibisyona sebep oldu. Metal iyonlarının meydana getirdiği aktivasyon EDTA ilavesiyle tamamen ortadan kalktı, Het'nin yaptığı inhibisyon üzerinde ise EDTA nın herhangibir etkisi tespit edilemedi.

Keywords

İNSAN ERİTROSİT ALDEHİT DEHİDROGENAZININ KISMEN SAFLAŞTIRILARAK KİNETİK ÖZELLİKLERİNİN İNCELENMESİ , insan , inceleme

Investıgatıon Of Kınetıc Propertıes Of Human Erythrocyte Aldehyde Dehydrogenase By Partıally Purıfıcatıon

Abstract

Human erythrocyte aldehyde dehydrogenase was partially purified and its kinetic properties were examined. It was determined that the enzyme behaved in accordance with Michaelis Menten kinetics with the used substrates. Approximately 50 inhibition occurred in the enzyme activity with 10 4M disulfiram. This inhibition was completely eliminated with the addition of 1 mM 8-mercaptoethanol, whereas reduced glutathione had no effect. It was observed that 1.5 mM Mg and Car caused 96 45.16 and 9 54.84 activation in the enzyme activity, respectively. 1.5 mM Hgt caused approximately 90.32 inhibition. The activation caused by metal ions was completely eliminated with the addition of EDTA, and no effect of EDTA could be detected on the inhibition caused by Het.

Keywords

INVESTIGATION OF KINETIC PROPERTIES OF HUMAN ERYTHROCYTE ALDEHYDE DEHYDROGENASE BY PARTIALLY PURIFICATION , human , examination

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