The mutual interference between the second-derivative bands of tyrosine and tryptophan in proteins has been evaluated in terms of the ratio r between two peak-to-peak distances. The r values have been found to be well related, although not linearly, to the tyrosine/ tryptophan ratio in both model co
Second-derivative spectroscopy of proteins: Studies on tyrosyl residues
β Scribed by Ciro Balestrieri; Giovanni Colonna; Alfonso Giovane; Gaetano Irace; Luigi Servillo
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 449 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Ionization of the phenolic group of N-acetyltyrosynamide has been studied using secondderivative spectroscopy. At pH 12.5 the second-derivative spectrum of the model compound revealed the presence of derivative bands in a spectral region (between 250 and 270 nm) where interference coming from other ultraviolet-absorbing chromophores is negligible. One of these peaks (260-nm peak) has been employed for the determination of tyrosyl groups in mixtures containing the aromatic amino acids.
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