๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Fluorescence of Proteins in 6-M Guanidine Hydrochloride : A Method for the Quantitative Determination of Tryptophan

โœ 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

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


A method for the measurement of the sedi
โœ Bruce W. Patterson; Verne N. Schumaker; Waldo R. Fisher ๐Ÿ“‚ Article ๐Ÿ“… 1984 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 421 KB

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

A fluorometric method for the determinat
โœ T. Sasaki; B. Abrams; B.L. Horecker ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 526 KB

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