The ultrastructure of the byssal apparatus of a mussel. V. Localization of collagenic and elastic components in the threads.

Ultrastructural and cytochemical studies have been carried out on the proximal part of byssus threads (TPP) in an attempt to localize collagenic and elastic components. The results show that TPP autoclaving followed by hot alkali treatment causes the extraction of about two-thirds of hydroxyproline and the parallel removal of most of the matrix, leaving filaments unaffected. Moreover the results of the staining reactions signaletic for elastic tissues indicate that TPP filaments contain glycoproteins with a reactivity similar to that of many invertebrate elastic tissues. On the basis of these morphological findings, it seems reasonable to suggest that collagen may be located in TPP matrix, while filaments could be responsible for the elastic properties.