✦ LIBER ✦

Fluorometric detection of tyrosine residues in peptides after reaction with nitroso-naphthol

✍ Scribed by R. Håkanson; A.L. Rönnberg; K. Sjölund

Book ID: 102629179
Publisher: Elsevier Science
Year: 1973
Tongue: English
Weight: 251 KB
Volume: 51
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(73)90509-5

No coin nor oath required. For personal study only.

✦ Synopsis

Nitrosonaphthol

reacts with tyrosine-containing peptides, yielding intensely fluorescent condensation products, probably benzphenoxazinone derivatives. The condensation products of tyrosine and angiotensin migrate much slower on a Sephadex G 25 column than do the native compounds, the retardation probably being caused by the increased aromaticity of the condensation products. These observations make it possible to purify and measure tyrosine-containing peptides.

📜 SIMILAR VOLUMES

Interaction of sulfate ion with a critic

Interaction of sulfate ion with a critical tyrosine residue in yeast phosphoglycerate kinase detected through the tetranitromethane reaction

✍ Michael C. Meyer; Edward W. Westhead 📂 Article 📅 1976 🏛 Elsevier Science 🌐 English ⚖ 343 KB

Determination of residual 2,4,5-T in veg

Determination of residual 2,4,5-T in vegetables by high performance liquid chromatography with ultraviolet and fluorometric detection after derivatization with 2-(2,3-naphthalimino)ethyl trifluoromethanesulfonate (NE-OTf)

✍ Nagata, Tomoko 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 276 KB 👁 1 views

2,4,5-T was extracted with acetone at below pH 1É0 and the extract was concentrated. After adding 100 g litre~1 sodium chloride solution to the residual solution, 2,4,5-T was extracted with ethyl acetate ] hexane (20 ] 80 by volume). The extract was evaporated to dryness and the residue was dissolve