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The tryptophane and cystine content of various proteins

โœ Scribed by D. Breese Jones; C.E.F. Gersdorff; O. Moeller


Publisher
Elsevier Science
Year
1925
Tongue
English
Weight
53 KB
Volume
199
Category
Article
ISSN
0016-0032

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๐Ÿ“œ SIMILAR VOLUMES


Single analysis for cysteine, cystine, a
โœ A.S. Inglis; D.T.W. McMahon; C.M. Roxburgh; H. Takayanagi ๐Ÿ“‚ Article ๐Ÿ“… 1976 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 564 KB

Quantitative analysis for cysteinyl, cystinyl and tryptophyl residues, as well as those of the more stable amino acids, may be made on a single column of an amino acid analyzer after acid hydrolysis of either soluble or insoluble proteins. The procedure involves determination of cysteinyl residues a

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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

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The total salt-extractable protein from seeds of important cultivated legumes and sunflower kernels has a tryptophan content ranging from 0.91% (bywt) for chickpea (Cicer arietinum) to 1.99% (bywt) for green gram (Vigna radiata). In species with substantial albumin fractions, the tryptophan content