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Data supporting the spectrophotometric method for the estimation of catalase activity.

ABSTRACT: Here we provide raw and processed data and methods for the estimation of catalase activities. The method for presenting a simple and accurate colorimetric assay for catalase activities is described. This method is based on the reaction of undecomposed hydrogen peroxide with ammonium molybdate to produce a yellowish color, which has a maximum absorbance at 374 nm. The method is characterized by adding a correction factor to exclude the interference that arises from the presence of amino acids and proteins in serum. The assay acts to keep out the interferences that arose from measurement of absorbance at unsuitable wavelengths.

SUBMITTER: Hadwan MH

PROVIDER: S-EPMC4707181 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Data supporting the spectrophotometric method for the estimation of catalase activity.

Hadwan Mahmoud Hussein MH Abed Hussein Najm HN

Data in brief 20151217

Here we provide raw and processed data and methods for the estimation of catalase activities. The method for presenting a simple and accurate colorimetric assay for catalase activities is described. This method is based on the reaction of undecomposed hydrogen peroxide with ammonium molybdate to produce a yellowish color, which has a maximum absorbance at 374 nm. The method is characterized by adding a correction factor to exclude the interference that arises from the presence of amino acids and ...[more]

PMID: 26862558

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Project description:Background2'-5' oligoadenylate synthetases (OAS) are interferon inducible enzymes that polymerizes ATP to 2'-5'-linked oligomers of adenylate (2-5As). As part of the innate immune response, these enzymes are activated by viral double stranded RNA or mRNAs with significant double stranded structure. The 2-5As in turn activate RNaseL that degrade single stranded RNAs. Three distinct forms of OAS exist in human cells (OAS1, 2 and 3) with each form having multiple spliced variants. The OAS enzymes and their spliced variants have different enzyme activities. OAS enzymes also play a significant role in regulating multiple cellular processes such as proliferation and apoptosis. Moreover, Single nucleotide polymorphisms that alter OAS activity are also associated with viral infection, diabetes and cancer. Thus detection of OAS enzyme activity with a simple spectrophotometric method in cells will be important in clinical research.ResultsHere we propose a modified coupled spectrophotometric assay to detect 2-5 oligoadenylate synthetase (OAS) enzyme activity in prostate cell lines as a model system. The OAS enzyme from prostate cancer cell lysates was purified using Polyinosinic: polycytidylic acid (poly I:C) bound activated sepharose beads. The activated OAS enzyme eluted from Sepharose beads showed expression of p46 isoform of OAS1, generally considered the most abundant OAS isoform in elutes from DU14 cell line but not in other prostate cell line. In this assay the phosphates generated by the OAS enzymatic reaction is coupled with conversion of the substrate 2-amino-6-mercapto-7-methylpurine ribonucleoside (methylthioguanosine, a guanosine analogue; MESG) to a purine base product, 2-amino-6-mercapto-7-methylpurine and ribose1-phosphate via a catalyst purine nucleoside phosphorylase (phosphorylase) using a commercially available pyrophosphate kit. The absorbance of the purine base product is measured at 360 nm. The higher levels of phosphates detected in DU145 cell line indicates more activity of OAS in this prostate cancer cell line.ConclusionThe modified simple method detected OAS enzyme activity with sensitivity and specificity, which could help in detection of OAS enzymes avoiding the laborious and radioactive methods.

Project description:The analysis of antioxidants in different foodstuffs has become an active area of research, which has led to many recently developed antioxidant assays. Many antioxidants exhibit inherent electroactivity, and, therefore, the use of electrochemical methods could be a viable approach for evaluating the overall antioxidant activity of a matrix of nutraceuticals without the need for adding reactive species. Green tea is believed to be a healthy beverage due to a number of therapeutic benefits. Catechin, one of its constituents, is an important antioxidant and possesses free radical scavenging abilities. The present paper describes the electrochemical properties of three screen-printed electrodes (SPEs), the first one based on carbon nanotubes (CNTs), the second one based on gold nanoparticles (GNPs) and the third one based on carbon nanotubes and gold nanoparticles (CNTs-GNPs). All three electrodes were modified with the laccase (Lac) enzyme, using glutaraldehyde as a cross-linking agent between the amino groups on the laccase and aldehyde groups of the reticulation agent. As this enzyme is a thermostable catalyst, the performance of the biosensors has been greatly improved. Electro-oxidative properties of catechin were investigated using cyclic voltammetry (CV) and differential pulse voltammetry (DPV), and these demonstrated that the association of CNTs with GNPs significantly improved the sensitivity and selectivity of the biosensor. The corresponding limit of detection (LOD) was estimated to be 5.6 × 10-8 M catechin at the CNT-Lac/SPE, 1.3 × 10-7 M at the GNP-Lac/SPE and 4.9 × 10-8 M at the CNT-GNP-Lac/SPE. The biosensors were subjected to nutraceutical formulations containing green tea in order to study their catechin content, using CNT-GNP-Lac/SPE, through DPV. Using a paired t-test, the catechin content estimated was in agreement with the manufacturer's specification. In addition, the relationship between the CNT-GNP-Lac/SPE response at a specific potential and the antioxidant activity of nutraceuticals, as determined by conventional spectrophotometric methods (DPPH, galvinoxyl and ABTS), is discussed in the context of developing a fast biosensor for the relative antioxidant activity quantification.

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Data supporting the spectrophotometric method for the estimation of catalase activity.

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Data supporting the spectrophotometric method for the estimation of catalase activity.

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