Isolation and characterization of collagen type I crosslink from skin: high-resolution NMR reveals diastereomers of hydroxylysinonorleucine crosslink
Author:
Funder
New ZealanMinistry of Business and Innovation
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Clinical Biochemistry,Biochemistry
Link
http://link.springer.com/article/10.1007/s00726-019-02708-3/fulltext.html
Reference47 articles.
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2. Bailey AJ, Peach CM (1968) Isolation and structural identification of a labile intermolecular crosslink in collagen. Biochem Biophys Res Commun 33(5):812–819. https://doi.org/10.1016/0006-291x(68)90233-7
3. Bailey AJ, Peach CM, Fowler LJ (1970) Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen. Isolation and characterization Biochem J 117(5):819–831. https://doi.org/10.1042/bj1170819
4. Basil-Jones MM, Edmonds RL, Cooper SM, Kirby N, Hawley A, Haverkamp RG (2013) Collagen fibril orientation and tear strength across ovine skins. J Agric Food Chem 61(50):12327–12332. https://doi.org/10.1021/jf4038375
5. Brownell AG, Veis A (1975) The intracellular location of the glycosylation of hydroxylysine of collagen. Biochem Biophys Res Commun 63(2):371–377. https://doi.org/10.1016/0006-291x(75)90698-1
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