Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils.

摘要: Beta2-microglobulin fibrils have been extracted from the femoral head of a patient who has under chronic haemodialysis for 11 years. The primary structure N-terminal portion protein and mass determination by electrospray spectrometry demonstrate that beta2-microglobulin, as water extraction procedure, was not glycated Asn17 deamidated. Limited proteolysis observed in more than 20% beta2-microglobulin molecules main cleavage sites were at C-terminus Lys6 Tyr10. purified gel filtration 6 M Gdn/HCl submitted to refolding procedure. conditions determined through study unfolding pathway native protein. is stable neutral pH where it displays lower tendency self-aggregate acidic conditions. Pulse dilution extensive dialysis buffer 7.5 yields with tertiary identical form. CD spectrum near-ultraviolet region intrinsic fluorescence Trp overlap those protein, but far-ultraviolet affected contribution oligomers created fragments reduce positive light polarisation 205 nm typical beta2-microglobulin.