“In Vitro” Fibril Formation of type I Collagen from Different Sources: Biochemical and Morphological Aspects

Acid soluble type I collagen was prepared from fetal and adult bovine tendon and skin and from adult bovine cornea. The degree of hydroxy lysine glycosylation and the hydroxy lysine di-to monoglycoside ratio as well as the “in vivo” fibril diameters, were shown to be tissue and age-dependent. Fibrils of type I collagen were reconstituted “in vitro” monitoring at 313 nm. The fibrils obtained were examined by electron microscopy. It was shown that the “in vitro” lateral growth of collagen fibrils leads to the formation of fibrils with maximum diameters which may be correlated to those of the corresponding native fibrils. Moreover it is suggested that one of the factors controlling the lateral growth of collagen may be at the level of hydroxy lysine glycosylation.