The identification of εN-(β-aspartyl)-l-lysine in native and heated keratin
✍ Scribed by R. S. Asquith; M. S. Otterburn; K. L. Gardner
- Book ID
- 112703103
- Publisher
- Springer
- Year
- 1971
- Tongue
- English
- Weight
- 249 KB
- Volume
- 27
- Category
- Article
- ISSN
- 1420-682X
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📜 SIMILAR VOLUMES
## Abstract The separation and resolution of the isopeptides __N__ϵ(γ‐glutamyl)‐L‐lysine and __N__ϵ(β‐aspartyl)‐L‐lysine formed in heated proteins has been successfully achieved. The method demands a well‐characterised ion‐exchange column and the use of pH 3.40 lithium citrate buffer (0.2 N Li^+^).
## Abstract Uncharged poly(__N__^ε^‐methyl‐L‐lysine) (PMLL) and its isomer, poly(__N__^δ^‐ethyl‐L‐ornithine) (PELO), in alkaline solution (pH ca. 12) undergo a helix‐to‐β transition upon mild heating at 50°C or higher in a manner similar to that of poly(L‐lysine) (PLL). The rate of conversion follo
From the reaction between L-lysine and formaldehyde, W-formyl-L-lysine was isolated by means of ion-exchange column chromatography. The identification of W-formyl-L-lysine was carried out by ion-exchange overpressured-layer chromatography (OPLC) and 'H NMR and 13C NMR spectroscopies. The m.p. and mi