نتایج جستجو برای: nitrophenyl

تعداد نتایج: 3814  

Journal: :European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies 1992
L Haagen A Brock

A new method for phenotyping human serum arylesterase (EC 3.1.1.2) is described and evaluated. The aromatic esters, phenyl acetate and 4-nitrophenyl acetate, were compared as substrates for spectrophotometric measurement of arylesterase activity. A method for arylesterase phenotyping, based upon inhibition of the enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate, was developed. Th...

Journal: :Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 2005
Giiltekin Gökce Zehra Durmuş Habibe Tezcan Esma Kiliç Hamza Yilmaz

Cyclic voltammetric (CV) and chronoamperometric (CA) behaviors of 1,3,5-triphenylformazan (TPF), 3-(p-nitrophenyl)-1,5-diphenylformazan (PNF) and 3-(m-nitrophenyl)-1,5-diphenylformazan (MNF) were studied in dimethyl sulfoxide medium. TPF was found to give a single sharp cathodic CV peak corresponding to a gain of one-electron per molecule. The diffusion coefficient and the number of electrons t...

Journal: :Bioscience, biotechnology, and biochemistry 1998
M Senba N Kashige F Miake K Watanabe

Three β-N-acetylglucosaminidases, GlcNAcase A, B, and C, were purified from the culture fluid of Lactobacillus casei ATCC 27092, and the molecular weights of these enzymes were estimated to be 54,000, 51,000, and 44,000, respectively, by SDS-PAGE. The production of these GlcNAcases was accelerated by the addition of N-acetylglucosamine to the culture. These enzymes had pIs of about 5.2, an opti...

Journal: :Journal of bacteriology 1969
F J Malveaux C L Clemente

At temperatures between 45 and 50 C, staphylococcal acid phosphatase purified 44-fold had maximal activity at pH 5.2 to 5.3. However, the enzyme was most stable in the alkaline range (pH 8.5 to 9.5) at temperatures below 50 C. Iodoacetate and ethylenediamine-tetraacetic acid were effective inhibitors, whereas mercaptoethanol and Cu(2+) acted as stimulators. The energy of activation for hydrolyt...

2017
Vinutha V. Salian Badiadka Narayana Balladka K. Sarojini

In the present investigation, the synthesis and spectroscopic characterization of N-(4-nitrophenyl)-2-{2-[3-(4-chlorophenyl)-5-[4-(propan-2-yl)phenyl]-4,5-dihydro-1H-pyrazol-1-yl]-4oxo-4,5-dihydro-1,3-thiazol-5-yl}acetamide (2) is performed. The title compound (2) is synthesized by the reaction of 3-(4-chlorophenyl)-5-[4-(propan-2-yl)phenyl]-4,5-dihydro-1H-pyrazole-1carbothioamide (1) with N-(4...

Journal: :Cancer research 1982
G B Whitehurst J P Mashburn T G Pretlow E L Bradley E A Boohaker

Hexosaminidase activity in prostatic tissue has been compared in 15 patients with benign prostatic hyperplasia and 15 patients with prostatic carcinoma. The ratio of enzymatic activity for the two substrates tested (p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside and p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside) was not significantly different in the two groups of patient...

Journal: :Dalton transactions 2012
Anand Pariyar Suranjana Bose Satyadeep Singh Chhetri Achintesh Narayan Biswas Pinaki Bandyopadhyay

Selective detection of Hg(II) ions in solution by a series of novel free base bis-(nitrophenyl) corroles (1-4) with general formula A(2)B (where A = nitrophenyl, and B = N,N-dimethylaminophenyl, thienyl, naphthyl and tridecyloxyphenyl group) is described. Among the free base corroles, 4, with a tridecyloxy long chain moiety, has been found to exhibit the highest Hg(II) sensing ability. The dete...

Journal: :Journal of Dairy Science 2021

A novel galactosidase gene (gal3149) was identified from Bacillus velezensis SW5 and heterologously expressed in Escherichia coli BL21 (DE3). The galactosidase, Gal3149, encoded by gal3149 an open reading frame of 1,299 bp, 433 amino acids length. Protein sequence analysis showed that Gal3149 belonged to family 4 glycoside hydrolases (GH4). displayed higher enzyme activity for the substrate 2-n...

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