Aorta Elasticae And Tendon Collagen Reactivity To 8-anilino-1-naphthalene Sulphate (ans) And Dansylchloride

Hydrophobicity and lysine richness were investigated in the elastic lamellae and binding elastic fibrils of the rat and human aortae and in the collagen fibers of the rat calcaneal tendons with microfluorometric methods (ANS-butanol and dansylchloride reactions, respectively). All the preparations treated with the ANS-butanol solution exhibited an emission peak at λ=470 nm. However, in this case, the fluorescence displayed by the elastic lamellae of the human aorta was deeper than that exhibited by the rat aorta. The binding elastic fibrils of the rat aorta, on the other hand, appeared more evident, in a large number, and more fluorescent than those of the human aorta. The collagen fibers fluoresced very pale with the ANS When treated with the dansylchloride, the collagen fibers appeared less fluorescent than the elastic lamellae and exhibited an emission peak at λ = 500 nm. The binding elastic fibrils practically did not fluoresce with the dansylchloride. The fluorescence of the rat elastic lamellae, on the other hand, was stronger than that of the human ones, both displaying, however, their emission peak positioned at λ=520-530 nm(filter set I) and λ= 600 nm (filter set IV). It is concluded that the binding elastic fibrils contain a larger amount of hydrophobic residues but lesser polarity than the elastic lamellae. The hydrophobicity of the binding elastic fibrils and elastic lamellae differs when comparing the human and rat aortae to each other.26658358