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Determination of cross-links in elastin

✍ Scribed by M. Ledvina; F. Bartoš

Publisher
Elsevier Science
Year
1967
Tongue
English
Weight
456 KB
Volume
31
Category
Article
ISSN
1873-3778

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✦ Synopsis

In 1963, during studies on the cross-links connecting the peptide chains in elastin, PARTRIDGE et al,19 2 discovered two hitherto unknown amino acids with a relatively high molecular weight in the elastic fibres; they designated them desmosine and isodesmosine. Their structure is as follows:

Desmosine is a tetraamino-tetracarbosylic acid with a quaternary pyridinium nitrogen. The ring can be built up by combination of one unchanged lysine with three lysine molecules oxidized to a-aminoaclipic semialdehyde, Isodesmosine is its isomer with the same substituents in the positions I, 2, 3 and 5.

In this paper, a method for the determination of desmosine and isodesmosine in elastin hydrolysates is described and discussed.

EXPERIMENTAL

Pvejbaration and hydrolysis of alastin

📜 SIMILAR VOLUMES

Separation and determination of cross-li
Separation and determination of cross-linking amino acids of elastin by high-voltage paper electrophoresis
✍ E. Moczar; B. Robert; L. Robert 📂 Article 📅 1972 🏛 Elsevier Science 🌐 English ⚖ 730 KB

## Purification of elastin can be accomplished by hydrolytic procedures using acids or alkali, enzymes, or autoclaving (l-3). The resulting preparations can be standardized and characterized only by their amino acid composition (1,4,5) and mainly by their desmosine and isodesmosine contents (6-9)