dc.contributor.author | Kulaksiz-Erkmen, Gulnihal | |
dc.contributor.author | Can, Betul | |
dc.contributor.author | Dalmizrak, Ozlem | |
dc.contributor.author | Ogus, I. Hamdi | |
dc.contributor.author | Ozer, Nazmi | |
dc.date.accessioned | 2019-12-16T07:57:23Z | |
dc.date.available | 2019-12-16T07:57:23Z | |
dc.date.issued | 2012 | |
dc.identifier.issn | 0354-4664 | |
dc.identifier.uri | https://doi.org/10.2298/ABS1201239E | |
dc.identifier.uri | http://hdl.handle.net/11655/19397 | |
dc.description.abstract | In this study we report on the effect of glycerol used in storage buffers, on the inhibitory kinetic behavior of NADP(+) on rat kidney glutathione reductase (rkGR) stored at -80 degrees C in +/- 10% (v/v) glycerol. At fixed [GSSG] and varied [NADPH], rkGR stored +/- glycerol were inhibited competitively by NADP(+). Although the addition of glycerol decreased K-m (9.7 +/- 0.9 mu M) and Ki(NADp+) (26.6 +/- 2.2 mu M) for NADPH, the catalytic efficiency (K-cat/K-m = 2.75 x 10(7) M-1.s(-1)) was increased 1.64 fold. At fixed [NADPH] and varied [GSSG], rkGR exhibited noncompetitive (K-i = 397 69 mu M) and linear mixed-type (K-i = 59.6 +/- 8.4 mu M; K-s = 49.9 +/- 3.2 mu M; alpha = 7.74) inhibitions with and without glycerol during storage. The K-cat/K-m of rkGR stored in glycerol was 5.16 x 10(6) M-1.s(-1). Although the increase in K-cat was 1.25 fold, the K-cat/K-m was minimally affected (1.06). | |
dc.language.iso | en | |
dc.publisher | Inst Bioloska Istrazivanja Sinisa Stankovic | |
dc.relation.isversionof | 10.2298/ABS1201239E | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | Life Sciences & Biomedicine - Other Topics | |
dc.title | The Effect of Glycerol in the Storage Medium on the Inhibitory Kinetic Behavior of Glutathione Reductase | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:eu-repo/semantics/publishedVersion | |
dc.relation.journal | Archives Of Biological Sciences | |
dc.contributor.department | Biyoloji | |
dc.identifier.volume | 64 | |
dc.identifier.issue | 1 | |
dc.identifier.startpage | 239 | |
dc.identifier.endpage | 247 | |
dc.description.index | WoS | |
dc.description.index | Scopus | |