Abstract
Solubilized proteins from avian epidermal structures are heterogeneous in sequence, share a common tertiary structure, and have similar tissue-specific molecular weights. The proteins, in the thiol (SH-) form, will self-associate in urea-free, neutral-pH, low-salt buffers and form tonofilaments indistinguishable from native filaments. The mechanics of these processes are similar to those of the α-keratins of various mammalian tissues, although the size and nature of the subunit, filament geometry, and relation to tissue morphology are different.
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