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Double beam spectrophotometer

Manufactured by Jasco
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Sourced in Japan

A double beam spectrophotometer is an instrument used to measure the absorption or transmission of light in a sample. It operates by splitting a beam of light into two separate beams, one of which passes through the sample and the other serves as a reference. The instrument then compares the intensity of the two beams and provides a measurement of the sample's absorbance or transmittance at different wavelengths of light.

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Lab products found in correlation

Close spelling variants of this product

V-530 double beam UV–VIS spectrophotometer (4 citations) V-650 UV-VIS double-beam spectrophotometer (3 citations) V-530 double beam spectrophotometer (3 citations) V-770 double-beam spectrophotometer (2 citations) V-560 double-beam spectrophotometer (2 citations) V-570 double beam spectrophotometer (2 citations) Jasco V-730 UV-Vis double-beam spectrophotometer (2 citations) UV-Vis V-550 double-beam spectrophotometer (2 citations)

2 protocols using double beam spectrophotometer

1

Spectrophotometric Analysis of Pharmaceutical Samples

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A double beam spectrophotometer (Jasco, Japan) was used for all spectrophotometric measurements. Spectrum treatment was achieved using Jasco spectra manager software. In pharmaceutical sample preparation, a sonicator (DAIHAN WUC-A01H, USA) has been used. Minitab 2019 was used in the statistical comparison survey for the results obtained and reported.
Ibrahim H., El-Abassy O.M., Abdellatef H.E., Hendawy H.A, & El-Sayed H.M. (2022). Simultaneous analysis of two drugs used as supportive treatment for COVID-19: comparative statistical studies and analytical ecological appraisal. BMC Chemistry, 16(1), 72.
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2

Lysozyme Aggregation Assay with sHSP Chaperone

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10 μM of lysozyme in 50 mM sodium phosphate buffer, pH 7.1, was denatured with 60 mM DTT at 37 °C. The aggregation of lysozyme was monitored for 20 minutes at 360 nm, in a JASCO double beam spectrophotometer. To assay chaperone activity of sHSPs, 10 μM of sHSP was added to the sample and reference cuvettes, prior to the addition of lysozyme in the sample cuvette. The chaperone activity of the separated fractions of the wild type protein were performed with 8 μM lysozyme denatured with 48 mM DTT. All other experimental conditions remained identical.
Mani N., Bhandari S., Moreno R., Hu L., Prasad B.V, & Suguna K. (2016). Multiple oligomeric structures of a bacterial small heat shock protein. Scientific Reports, 6, 24019.
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