Spectroscopic studies on pepsin-solubilized vitreous and cartilage collagens.

Circular dichroism and the fluorescent probe, 2-p-toluidinyl-naphthalene-6-sulfonate, were used to compare the molecular properties of pepsin-solubilized vitreous collagen with cartilage and calfskin collagens. Type II vitreous and cartilage collagens have more hydrophobic regions along their molecular domain than does type I calfskin collagen. The rate of fibril growth is faster in type II collagens than in type I. The increased hydrophobicity of type II collagens is attributed to high carbohydrate content and compositional variations. Although the secondary structures of the three collagens do not differ significantly, differences in carbohydrate content, composition, and hydrophobic character may cause some variations in the tertiary structures. It is suggested that the tertiary structure plays an important role in the nature and rate of fibril growth. Differences between cartilage and vitreous collagen in fluorescence behavior, fibril growth, and melting temperature indicate that vitreous collagen may be a "special type II collagen."