A rapid and inexpensive assay for dye-binding proteins has been developed. It depends on the separation of free and protein-bound sulfobromophthalein in I-ml columns of Sephadex G-25 due to differential adsorption of the dye to the protein and to the Sephadex. With bovine serum albumin the calibrati
A low cost nuclear technique for the rapid determination of the protein content of rice
โ Scribed by M. Hussain; M. Hoque
- Publisher
- Elsevier Science
- Year
- 1988
- Weight
- 216 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0883-2889
No coin nor oath required. For personal study only.
โฆ Synopsis
An attempt has been made to use the 10.82 MeV ;' rays emitted in the prompt "'N (n, ;!) reaction to investigate the feasibility of determining the content of nitrogen in bulk samples of rice using a '52Cf source. Gamma ray spectra of samples of urea (H,NCONH>) irradiated with thermal neutrons from a 2T2Cf source with a yield of 3.0 x 10' neutrons/s clearly showed the full energy peak and escape peaks due to y-rays from neutron capture in nitrogen. A 3 x 3 in. NaI(TI) crystal was used as the detector and the neutrons were thermalized in paraffin before their capture. The 10.82 Mev y-rays from neutron irradiated rice have been detected using the weak neutron source. It appears that the method should be useful for rapid determination of the nitrogen content in rice if a stronger californium source were employed. This should enable a rapid determination of the protein content. as this is correlated with the amount of nitrogen in the rice.
๐ SIMILAR VOLUMES
This study was conducted to assess the relative accuracy of five different assay techniques for the determination of protein concentration in human mixed saliva. The protein concentration of paraffin-stimulated saliva from 20 individuals was determined using the biuret reaction, the Lowry assay, a m
Digestion of proteins with a mixture of chymotrypsin and pronase followed by dilution in 6 M urea eliminates the quenching effects usually observed when tryptophan fluorescence is measured in native or denatured proteins. Following proteolysis, the tryptophan content can be estimated from the fluore
A simple and inexpensive method for determination of vlbratlonal transition moment directions in infrared spectroscopy is presented. The technique is based on the alignment of molecules in squeezed polyethylene sheets and the spectra are recorded with natural light. In many cases the method is able