A study on reconstitution methodology and influence ofin vitromaturation
- 1 January 1981
- journal article
- research article
- Published by Taylor & Francis in Connective Tissue Research
- Vol. 9 (1) , 51-57
- https://doi.org/10.3109/03008208109160239
Abstract
Acid extracted collagen from rat skin was reconstituted into fibrils at physiological pH and ion concentration. The fibrils were indistinguishable from native collagen in ultrastructural appearance. This report describes a procedure for reconstituting collagen fibrils into thin membranes which allows the preparation of a set of collagen membranes with identical mechanical properties. Reconstituted collagen fibrils showed a gain in mechanical strength upon maturation in vitro similar to the increase in mechanical strength known to occur during maturation of collagenous tissues in vivo. It is suggested that the changes in the mechanical properties of reconstituted collagen fibrils during in vitro maturation may reflect the changes observed during in vivo maturation of collagenous tissues. The possible influence of the amounts of reducible intermolecular cross-links on the gain in strength during maturation is discussed.This publication has 23 references indexed in Scilit:
- Changes in crosslinking during aging in bovine tendon collagenFEBS Letters, 1979
- Influence of Maturation and Age on Mechanical and Biochemical Parameters of Connective Tissue of Various Organs in the RatConnective Tissue Research, 1978
- Oxygen participation in the in vivo and in vitro aging of collagen fibresBiochemical and Biophysical Research Communications, 1977
- Some observations on the ageing in vitro of reprecipitated collagen fibresBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Biological significance of the intermolecular crosslinks of collagenNature, 1974
- Age‐related changes in the reducible crosslinks of human tendon collagenFEBS Letters, 1974
- Non‐helical regions in rat collagen α1‐chainFEBS Letters, 1972
- Age related changes in the reducible cross‐links of collagenFEBS Letters, 1971
- Evidence for a non‐helical region at the carboxyl terminus of the collagen moleculeFEBS Letters, 1971
- Isolation and Properties of a Collagen soluble in Salt Solution at Neutral pHNature, 1955