Biyoteknoloji BölümüBiyoteknoloji Bölümü'ne ait koleksiyonları içerir.http://hdl.handle.net/11772/5532024-03-28T08:24:36Z2024-03-28T08:24:36ZProduction of red fluorescent protein (mCherry) in an inducible E. coli expression system in a bioreactor, purification and characterizationKuduğ, HülyaAtaman, Bahadırİmamoğlu, RizvanDüzgün, DuyguGökçe, İsahttp://hdl.handle.net/11772/16562019-07-17T00:00:20Z2018-06-01T00:00:00ZProduction of red fluorescent protein (mCherry) in an inducible E. coli expression system in a bioreactor, purification and characterization
Kuduğ, Hülya; Ataman, Bahadır; İmamoğlu, Rizvan; Düzgün, Duygu; Gökçe, İsa
New and improved genetic engineered variants of fluorescent proteins (FPs) have become useful tools for bioimaging in biomedical researches. Red fluorescent proteins (RFPs) first derived from the sea anemone Discosoma show high performance in vivo labeling and imaging. mCherry is a member of RFPs which has very high photostability, resistant to photo bleaching and rapid maturation. These advantages ensure that mCherry can be successfully fused to many proteins and widely used for quantitative imaging techniques. In this study, the constructed recombinant plasmid pBADCherry was expressed in Escherichia coli BL21(AI) then culture conditions, inducer concentration and induction time were optimized. Results of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis demonstrated that 5 hours induction at 0.04% of arabinose concentration was optimal for the highest mCherry yield. The expression of
hexa histidine-tagged (6xHis) recombinant mCherry was induced by arabinose and purification
performed using nickel (Ni2+) affinity chromatography. High throughput expression of 81 mg
fluorescent protein from a liter of E. coli culture carried out in bioreactor.
2018-06-01T00:00:00ZSynthesis of some tetrahydropyrimidine-5-carboxylates, determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, butyrylcholinesterase and carbonic anhydraseSujayev, AfsunGaribov, EminTaslimi, ParhamGulcin, IlhamiGojayeva, SevinjFarzaliyev, VagifAlwasel, Saleh H.Supuran, Claudiu T.http://hdl.handle.net/11772/13922019-06-13T07:03:48Z2016-01-01T00:00:00ZSynthesis of some tetrahydropyrimidine-5-carboxylates, determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase
Sujayev, Afsun; Garibov, Emin; Taslimi, Parham; Gulcin, Ilhami; Gojayeva, Sevinj; Farzaliyev, Vagif; Alwasel, Saleh H.; Supuran, Claudiu T.
2-(Methacryloyloxy)ethyl 6-methyl-2-oxo-4-phenyl-1,2,3,4-tetrahydropyrimidine-5-carboxylate, is a cyclic urea derivative synthesized from urea, 2-(methacryloyloxy) ethyl acetoacetate and substituted benzaldehyde, and tested in terms of the inhibition of two physiologically relevant carbonic anhydrase (CA) isozymes I and II. Acetylcholinesterase (AChE) is found in high concentrations in the red blood cells and brain. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Also, they were tested for the inhibition of AChE and BChE enzymes and demonstrated effective inhibition profiles with Ki values in the range of 429.24-530.80 nM against hCA I, 391.86-530.80 nM against hCA II, 68.48-97.19nM against AChE and 104.70-214.15 nM against BChE. On the other hand, acetazolamide clinically used as CA inhibitor, showed Ki value of 281.33 nM against hCA I, and 202.70 nM against hCA II. Also, Tacrine inhibited AChE and BChE showed Ki values of 396.03 and 209.21 nM, respectively.
2016-01-01T00:00:00ZInhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesteraseOzgun, Dilan OzmenYamali, CemGul, Halise InciTaslimi, ParhamGulcin, IlhamiYanik, TelatSupuran, Claudiu T.http://hdl.handle.net/11772/13912019-06-13T07:01:30Z2016-01-01T00:00:00ZInhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesterase
Ozgun, Dilan Ozmen; Yamali, Cem; Gul, Halise Inci; Taslimi, Parham; Gulcin, Ilhami; Yanik, Telat; Supuran, Claudiu T.
The effects of isatin Mannich bases incorporating (1-[piperidin-1-yl (P1)/morpholin-4-yl (P2)/N-methylpiperazin-1-yl (P3)]methyl)-1H-indole-2,3-dione) moieties against human (h) carbonic anhydrase (CA, EC 4.2.1.1) isoenzymes hCA I and hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes were evaluated. P1-P3 demonstrated impressive inhibition profiles against AChE and BChE and also inhibited both CAs at nanomolar level. These inhibitory effects were more powerful in all cases than the reference compounds used for all these enzymes. This study suggests that isatin Mannich bases P1-P3 are good candidate compounds especially for the development of new cholinesterase inhibitors since they were 2.2-5.9 times better inhibitors than clinically used drug Tacrine.
2016-01-01T00:00:00ZThe human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivativesTaslimi, ParhamGulcin, IlhamiOzgeris, BunyaminGoksu, SuleymanTumer, FerhanAlwasel, Saleh H.Supuran, Claudiu T.http://hdl.handle.net/11772/13902019-06-13T06:55:21Z2016-01-01T00:00:00ZThe human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivatives
Taslimi, Parham; Gulcin, Ilhami; Ozgeris, Bunyamin; Goksu, Suleyman; Tumer, Ferhan; Alwasel, Saleh H.; Supuran, Claudiu T.
Carbonic anhydrases (CAs, EC 4.2.1.1) had six genetically distinct families described to date in various organisms. There are 16 known CA isoforms in humans. Human CA isoenzymes I and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. Acetylcholine esterase (AChE. EC 3.1.1.7) is a hydrolase that hydrolyzes the neurotransmitter acetylcholine relaying the signal from the nerve. In this study, some trimethoxyindane derivatives were investigated as inhibitors against the cytosolic hCA I and II isoenzymes, and AChE enzyme. Both hCA isozymes were inhibited by trimethoxyindane derivatives in the low nanomolar range. These compounds were good hCA I inhibitors (Kis in the range of 1.66-4.14nM) and hCA II inhibitors (Kis of 1.37-3.12nM) and perfect AChE inhibitors (Kis in the range of 1.87-7.53nM) compared to acetazolamide as CA inhibitor (Ki: 6.76nM for hCA I and Ki: 5.85nM for hCA II) and Tacrine as AChE inhibitor (Ki: 7.64nM).
2016-01-01T00:00:00Z