Thyroxine-binding Prealbumin
1971; Elsevier BV; Volume: 246; Issue: 19 Linguagem: Inglês
10.1016/s0021-9258(18)61827-7
ISSN1083-351X
AutoresWilliam Branch, Jacob Robbins, Harold Edelhoch,
Tópico(s)Bone health and treatments
ResumoAbstract Thyroxine-binding prealbumin (TBPA) has a molecular weight of 54,000 in aqueous solution and dissociates into 4 subunits of identical size in 6 m guanidine. From the far ultraviolet circular dichroic spectra, about half of the peptide groups were estimated to form β structures and the other half to be essentially unordered. The internal organization of TBPA appears not to change between pH 12 and 3.5. There is a structural transition between pH 3.5 and 2.5 which involves exposure of all of the buried aromatic chromophores. TBPA is not dissociated in strong acid or alkali or in 0.1% sodium dodecyl sulfate.
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