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Rapid separation and analysis of Nϵ-(γ-glutamyl)-L-lysine-and Nϵ-(β-aspartyl)-L-lysine in protein digests

✍ Scribed by Michael S. Otterburn; William J. Sinclair

Publisher
John Wiley and Sons
Year
1976
Tongue
English
Weight
396 KB
Volume
27
Category
Article
ISSN
0022-5142

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✦ Synopsis

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^+^). Due to the variations in particle size and cross‐linkages in the ion‐exchange resin a computer‐assisted buffer gradient system has been developed. This system effects resolution of both isopeptides in 7 h. The use of leucyl‐glycine as an internal standard facilitates quantitative estimation of the isopeptides.

📜 SIMILAR VOLUMES

Conformational change of poly-Nε-glutary
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## Abstract The conformational changes of poly‐__N__^ε^‐glutaryl‐L‐lysine (PGL) and poly‐__N__^ε^‐succinyl‐L‐lysine (PSL) in various salt solutions were studied by use of ORD and potentiometric titration measurements. The addition of alkali metal salts to the fully ionized PGL or PSL solution cause

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✍ Hiroyuki Yamamoto; Jen Tsi Yang 📂 Article 📅 1974 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 380 KB 👁 1 views

## 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