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Separation of the cross-linking amino acids of elastin on thin-layer plates
Ist Teil von
Journal of Chromatography A, 1984, Vol.305 (2), p.461-464
Ort / Verlag
Amsterdam: Elsevier B.V
Erscheinungsjahr
1984
Quelle
Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
Beschreibungen/Notizen
There has long been a need for a simple and rapid method of separating the cross-linking amino acids of elastin. Such a procedure would greatly assist both structural and metabolic studies of this important protein, which is present in most types of connective tissue. The previously reported TLC procedure separates all four cross-links from one another but is not able to separate the cross-links from certain other amino acids, as lysine, arginine and proline. To resolve this problem the authors have now devised a two-dimensional TLC procedure which completely separates the four cross-linking amino acids from each other and from all other amino acids present in elastin hydrolyzates.