نتایج جستجو برای: km and vmax

تعداد نتایج: 16830427  

2017
Narin Kirikyali Jonathan Wood Ian F Connerton

β-xylosidases catalyse the hydrolysis of short chain xylooligosaccharides from their non-reducing ends into xylose. In this study we report the heterologous expression of Aspergillus oryzae β-xylosidase (XylA) in Pichia pastoris under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter. The recombinant enzyme was optimally active at 55°C and pH 4.5 with Km and Vmax values of 1....

Journal: :Drug metabolism and disposition: the biological fate of chemicals 2006
Ryan W Dellinger Jia-Long Fang Gang Chen Rebecca Weinberg Philip Lazarus

UDP-glucuronosyltransferase 1A10 (UGT1A10) is an extrahepatic enzyme expressed in aerodigestive tract tissues that exhibits significant glucuronidation activity against the important procarcinogenic benzo(a)pyrene (BaP) metabolite, BaP-trans-7,8-dihydrodiol (BPD), and the UGT1A10 codon 139 (Glu>Lys) polymorphism was previously implicated in risk for orolaryngeal cancer by Elahi et al. in their ...

2002
Philippe Amram

We use Fabry-Perot Hα spectroscopy, complemented with published H I radio synthesis observations to derive high resolution rotation curves of spiral galaxies. We investigate precisely their inner mass distribution and compare it to CDM simulations predictions. Having verified the existence of the so-called core-cusp problem, we find that the dark halo density inner slope is related to the galax...

Journal: :Cancer research 1987
D Wade C S Yang C J Metral J M Roman J A Hrabie C W Riggs T Anjo L K Keefer B A Mico

In an attempt to elucidate the molecular basis for the decrease in rat liver carcinogenicity and DNA-alkylating ability that accompanies deuteration of N-nitrosodimethylamine (NDMA), NDMA and its fully deuterated analogue ([2H6]NDMA) were incubated with acetone-induced rat liver microsomes. Rates for the competing metabolic routes, denitrosation and demethylation, were determined from colorimet...

Journal: :molecular biology research communications 2013
sona talaei asadollah asadi mojtaba amani

copper amine oxidases (caos) catalyse the oxidative de-amination of biogenic amines which are ubiquitous compounds essential for cell growth and proliferation. the enzymes are homodimers containing both topaquinone and a cu(ii) ions as cofactors at the active site of each subunit. after extraction and purification of chickpea (cicer arietinum) amine oxidase by chromatoghraphy, km and vmax of th...

Journal: :Toprak Bilimi ve Bitki Besleme Dergisi 2022

Çalışmada, toprağın katalaz enziminin kinetik parametrelerini (Vmax, KM, Vmax/KM, KSEE, [S]opt ve υ0,max) hesaplamak için H2O2 substratının farklı konsantrasyonlarında (3, 6, 9, 12, 15, 18, 21, 24, 30 %) analizler yapılmıştır. Bu parametrelerin hesaplanması analiz sonuçları kullanılarak önce hız (υ) değerleri hesaplanmıştır. Sonra ürün – substrat: [P]=f([S]) bağıntısını ifade eden modeller beli...

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه فردوسی مشهد - دانشکده علوم 1390

آنزیم آلفا آمیلاز در حضور کربودی ایمید، به صورت مستقیم بر روی نانوذرات مغناطیسی fe3o4 تثبیت شد. نتایج بدست آمده نشان داد که بازده فرآیند تثبیت و میزان فعالیت باقیمانده آنزیم آمیلاز تثبیت شده به دمای تثبیت و نسبت جرمی نانوذره: کربودی ایمید: آلفا آمیلاز بستگی دارد. اثر عوامل مختلف مانند دما و ph بر آنزیم آمیلاز تثبیت شده بررسی شد و با آنزیم آمیلاز محلول مقایسه شد. ph بهینه برای آنزیم آمیلاز محلول...

Journal: :Biochemical Society transactions 1990
G M Lawrence A C Beesley G I Mason J B Matthews

Journal: :The Journal of biological chemistry 1981
J A Idell-Wenger

The kinetic behavior of the carnitine:acylcarnitine translocase was studied in isolated rat heart mitochondria. The kinetic parameters, Km(apparent) and Vmax, for carnitine were determined by measuring the rates of influx of [14C]carnitine using two different methods to quench the exchange reaction. The range of the Km(app) was 0.38-1.50 mM and the Vmax was 0.20-0.34 nmol/mg . min by both metho...

Journal: :Journal of applied physiology 2001
J W Rush L L Spriet

This study aimed to determine physiologically relevant kinetic and allosteric effects of P(i), AMP, ADP, and caffeine on isolated skeletal muscle glycogen phosphorylase a (Phos a). In the absence of effectors, Phos a had Vmax = 221 +/- 2 U/mg and Km = 5.6 +/- 0.3 mM P(i) at 30 degrees C. AMP and ADP each increased Phos a Vmax and decreased Km in a dose-dependent manner. AMP was more effective t...

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