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Öğe Effect of bovine serum albumine on production of ?-amylase and amylase thermostability in Bacillus subtilis(1997) Otludil B.; Ensari N.Y.; Aguloglu S.; Uyar F.Thermal stability of ?-amylase from Bacillus subtilis isolated from thermal Cermik hot spring was studied ?-amylase was purified from media with and without bovine serum albumen (BSA). The enzyme was stable at 68°C when purified from media with different concentrations of BSA; however, it was observed to be stable at 75°C when interacted with different concentrations of BSA. B. subtilis was grown in different concentrations of BSA. The best bacterial growth was identified to be in the medium with 180 ?g/ml BSA. Production of ?-amylase and proteases was induced in presence of 180-240 ?g/ml BSA.Öğe The formation of callus cultures from unpollinated pistils in cotton plant (Gossypium hirsutum L.)(1998) Taskin T.; Demir R.; Otludil B.In this study, unpollinated floral buds of cotton (Gossypium hirsutum L.) were cultured on the Murashige and Skoog (MS) media containing Kinetin (Kin) and Indol Asetic Acid (IAA) at different concentrations for the callus cultures. The nutrient medium containing 2 mg/l Kin + 1 mg/l IAA was observed to be the best medium for the callus formation from ovule and ovarium tissues.Öğe Intravesical oxybutynin application: Ultrastructural effects on bladder epithelium(1999) Ersay A.; Ketani M.A.; Nergiz Y.; Demirtas O.C.; Akkus M.; Otludil B.Intravesically applied oxybutynin, rapidly absorbs into the bloodstream, additional to profound local effect. Currently morphologic effects of oxybutynin on local bladder tissue relatively well established at light microscopic level, but not ultrastructural level. Thirty New Zealand White female rabbits were catheterized daily and intravesical instillation were performed with whether l mg/kg oxybutynin solution or saline for 30 days. The local effects of the drug on bladder epithelium at electron microscopic level were examined comparing with saline administration. Urinary tract infection (UTI) incidence were similar in both saline and oxybutynin groups (9 vs. 10 of 15 animals respectively) (p>0.05). Interestingly, in 4 of 5 animals that received oxybutynin and never had UTI during the study, separation of zonula occludens intercellular junction was determinated by Jeol electron microscope. This observation can explain rapid absorption of oxybutynin through the bladder into the blood stream. Oxybutynin can damage bladder surface epithelium at ultrastructural level. This effect may lead to increase absorption of it, but not result in higher incidence of bacterial infection.Öğe Polyphenol oxidase activity during rooting in cuttings of grape (Vitis vinifera L.) varieties(2003) Yilmaz H.; Taşkin T.; Otludil B.Polyphenol oxidase (PPO) activity was investigated during rooting in cuttings from three different grape cultivars (Vitis vinifera L. cvs. Muscat, Cardinal and Perlelte), and the enzyme activity and rooting ability were compared. Rooting was observed on the Muscat and Perlelte cuttings, but not on the Cardinal cuttings. PPO activity started to increase in the early stage of the experiment, and decreased after root emergence in the Muscat and Perlelte cuttings. However, enzyme activity started to increase in the early stages and continued throughout the experiment in the Cardinal cuttings. No apparent correlation was found between PPO activity and rooting ability in the cutting.Öğe Purification and characteristics of alkaline proteinase from alkalophylic Bacillus sp.(2001) Muderrizade A.; Ensari N.Y.; Aguloglu S.; Otludil B.Alkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degrees C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37 degrees C for 30 min. The optimum pH was 11.5 at 37 degrees C and the optimum temperature was 62 degrees C at pH 11.5.Öğe Purification and characterization of alkaline protease from alkalophilic Bacillus sp.(2001) Muderriszade A.; Ensari N.Y.; Aguloglu S.; Otludil B.Alkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37°C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37°C for 30 min. The optimum pH was 11.5 at 37°C and the optimum temperature was 62°C at pH 11.5.
