نتایج جستجو برای: ammonium hydrolysis

تعداد نتایج: 62850  

1995
James R. Christian David M. Karl

Ectoenzymatic hydrolysis is a crucial first step in bacterial utilization of polymeric dissolved organic matter (DOM). Variation in the relative activities of different enzymes can indicate seasonal and geographic variation in the mode of bacterioplankton nutrition. We found that relative activities of leucine aminopeptidase and P-glucosidase in seawater varied significantly among three oceanic...

Journal: :Journal of bacteriology 1968
G A Somkuti F J Babel

The protease produced by Mucor pusillus was recovered from a wheat bran medium by treatment with ammonium sulfate, ethyl alcohol, gel filtration and ion-exchange chromatography. The yield of the enzyme was 55%. The overall increase in the specific activity of the protease was 34-fold. The purified protease was most active at pH 3.8 and 5.6 against hemoglobin and casein, respectively. Optimal hy...

Journal: :Acta poloniae pharmaceutica 2014
Przemysław Zalewski Judyta Cielecka-Piontek Magdalena Paczkowska

A stability-indicating LC assay method was developed and validated for a simultaneous determination of meropenem and potassium clavulanate in the presence of degradation products formed during acid-base hydrolysis, oxidation and thermolysis. The isocratic RP-HPLC method was developed with a LiChrospher RP-18 (250 mm x 4.6 mm, 5 microm) column and gradient elution of 12 mmol/L ammonium acetate a...

2014
M. MATHRUSRI ANNAPURNA A. NARENDRA ALOK SAHU

A simple stability-indicating RP-HPLC method has been developed and validated for the determination of Racecadotril (RAC) in pharmaceutical dosage forms. The mobile phase consisting of methanol and tetra butyl ammonium hydrogen sulphate (80: 20, v/v) was used using isocratic elution with UV detection at 230 nm. The method showed good linearity for RAC in the 5-120 μg/mL range being the square o...

Journal: :Acta crystallographica. Section D, Biological crystallography 2002
Edward J Hollingsworth Michail N Isupov Jennifer A Littlechild

The enzyme L-aminoacylase catalyses the hydrolysis of N-acyl-L-amino acids from peptides or proteins. The recombinant enzyme from the hyperthermophilic archaeon Thermococcus litoralis has been purified to homogeneity. This zinc-containing enzyme has been crystallized from ammonium sulfate using the sitting-drop vapour-diffusion method. The crystals diffract to 2.8 A resolution and belong to the...

Journal: :The Journal of biological chemistry 1981
G W Cyboron R E Wuthier

Alkaline phosphatase has been purified from microsomes of chicken epiphyseal cartilage by first selectively extracting certain adventitious proteins with 0.25 M trichloroacetate. The membrane-bound enzyme was then solubilized by 1% cholate in buffered 33% saturated ammonium sulfate and purified by column chromatography on Bio-Gel A-5m, extraction with 1-butanol, and ion exchange chromatography ...

Journal: :Applied and environmental microbiology 2001
Y Sanz F Toldrá

An X-prolyl-dipeptidyl peptidase has been purified from Lactobacillus sakei by ammonium sulfate fractionation and five chromatographic steps, which included hydrophobic interaction, anion-exchange chromatography, and gel filtration chromatography. This procedure resulted in a recovery yield of 7% and an increase in specificity of 737-fold. The enzyme appeared to be a dimer with a subunit molecu...

Journal: :The Journal of biological chemistry 1967
J D Schnatz J A Cortner

Neutral lipolytic activity (hydrolysis of olive oil at 37”, pH 7.0) and alkaline lipolytic activity (hydrolysis of tributyrin at 47’, pH 8.0) have previously been demonstrated in human adipose tissue. Neutral lipolytic activity has currently been shown to be present in a large molecular weight substance, associated with lipid, and separable from most alkaline lipolytic activity by ammonium sulf...

Journal: :The Journal of biological chemistry 1983
C T Wittwer D Burkhard K Ririe R Rasmussen J Brown B W Wyse R G Hansen

A microsomal glycoprotein that catalyzes the hydrolysis of pantetheine to pantothenate and cysteamine was solubilized and purified to homogeneity as determined by sodium dodecyl sulfate electrophoresis. The enzyme from pig kidney cortex was solubilized on exposure to butanol and purified by heat treatment, ammonium sulfate fractionation, hydrophobic chromatography, and hydroxyapatite chromatogr...

2005
M. Hutnan M. Drtil J. Derco L. Mrafkova

Due to its structure, hexamethylenetetramine (HMT) is a slowly biodegradable substance, hydrolysing in acid environment to ammonium and formaldehyde. Formaldehyde is toxic under normal conditions for biological treatment processes. Following an adaptation, a formaldehyde concentration of 1000 mg·l may become biodegradable both in aerobic and anaerobic conditions. Acidic conditions for hydrolysi...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید