Thioflavin S binds non-amyloid protein structures in lampbrush chromosomes of <em>Gallus gallus domesticus</em>

Proteins that normally function in amyloid form are found bacteria, yeast, plants and vertebrates, including humans. In particular, fibrils amyloid-like structures described the germ cells of various organisms. Recently we showed chicken oocytes there some nuclear stained by amyloid-specific dye thioflavin S. Here demonstrate S binds giant terminal RNP aggregates lampbrush chromosomes. However, these not with Congo red conformation-dependent anti-amyloid antibodies. Thus, stains chromosome-associated proteins do have properties. These data indicate must be used caution when identifying new functional pathological amyloids.