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Cross-linking of dermal sheep collagen using a water-soluble carbodiimide [PDF]
Biomaterials, 1996 A cross-linking method for collagen-based biomaterials was developed using the water-soluble carbodiimide 1-ethyl-3-(3-dimethyl aminopropyl)carbodiimide hydrochloride (EDC).
Marja van Luyn +2 more
exaly +3 more sources
Collagen and Related Research, 1982
The structural macromolecules of the extracellular matrix have been investigated with rapidly increasing activity and depth in the past decade. Collagen, and to a lesser extent, elastin, were among the earliest of this group to be studied in more detail than the proteoglycans and adhesive glycoproteins.
M L, Tanzer, J H, Waite
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The structural macromolecules of the extracellular matrix have been investigated with rapidly increasing activity and depth in the past decade. Collagen, and to a lesser extent, elastin, were among the earliest of this group to be studied in more detail than the proteoglycans and adhesive glycoproteins.
M L, Tanzer, J H, Waite
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CROSS-LINKING IN COLLAGEN AND ELASTIN
Annual Review of Biochemistry, 1984PERSPECTIVES AND SUMMARy 717 LYSYL OXIDASE 719 COLLAGEN 720 Allysine and Hydroxyallysine Pathways 720 Hydroxypyridinium Residues... ... 724 Molecular Sites 730 Basement Membranes 733 Methods oj Analysis 734 Alternative M echanisms ...
D R, Eyre, M A, Paz, P M, Gallop
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The timecourse of collagen cross-linking
Biochimica et Biophysica Acta (BBA) - General Subjects, 1974Abstract The incorporation of [ 3 H] proline into all major denaturation subunits of acid-extractable skin collagen was followed in vivo over a period of 30 days in young male rats. The radioactivity was incorporated into the α 1 and α 2 subunits at an equal rate.
J S, Pinto, J P, Bentley
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Microwave irradiation and cross-linking of collagen
Biomaterials, 1992In a multifactorial experiment, dermal sheep collagen was treated in diluted glutaraldehyde solutions, 70% ethyl alcohol, Cialit 1:5000, and distilled water for 1, 3 and 5 min, respectively, in combination with microwave irradiation at different temperature settings.
Visser, C. E. +4 more
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Science (New York, N.Y.), 1973
The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the ...
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The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the ...
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The effects of copper on collagen cross-linking
Biochemical and Biophysical Research Communications, 1969Abstract Evidence in this report indicates that copper is directly involved in the process of collagen cross-linking. The bones from chicks fed copper-deficient diets became brittle and fragile. The collagen in copper-deficient bone was more easily extracted and contained less total aldehyde than corresponding controls.
R B, Rucker, H E, Parker, J C, Rogler
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Lysine Hydroxylation and Cross-Linking of Collagen
2019Collagens represent a large family of structurally related proteins containing a unique triple-helical structure. Among them, the fibril-forming collagens are the most abundant in vertebrates providing tissues with form and stability. One of the characteristics of the fibrillar collagens is its sequential posttranslational modifications of specific ...
Mitsuo, Yamauchi +2 more
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Collagen cross-linking in bovine gingiva
Archives of Oral Biology, 1991Tissue samples from 5 different sites of 6 bovine mandibles were used to quantify collagen cross-links as moles cross-link per mole of collagen. Gingiva contained primarily 3 reducible cross-links, deH-DHLNL, deH-HHMD, and deH-HLNL, and relatively small amounts of non-reducible cross-links.
J H, Tanner, M, Yamauchi, D M, Simpson
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