Fluorescence of Proteins in 6-M Guanidine Hydrochloride : A Method for the Quantitative Determination of Tryptophan
โ Scribed by Patrick PAJOT
- Book ID
- 115115261
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 651 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1432-1327
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๐ SIMILAR VOLUMES
A technique has been perfected for measuring the sedimentation coefficient of microgram quantities of a reduced protein in 6 M guanidine hydrochloride. The protein is sedimented through a gradient of 5-8 M guanidine-HCl in the presence of dithiothreitol in a SW 50.1 swinging-bucket rotor. Run condit
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