Hydrophobic properties of an amyloidogenic kappa I-Bence Jones protein fragment in charge shift electrophoresis.
Increase in hydrophobicity of amyloid-A protein as compared to the serum amyloid-A precursor protein has been demonstrated with charge shift electrophoresis. Charge shift electrophoresis was applied to the kappa-Bence Jones protein MEV, to amyloid-like fibrils generated in vitro by limited proteolysis of MEV and to an isolated, naturally occurring isolated A lambda (ULI) amyloid fibril protein, to see whether an increase in hydrophobicity is also found in to the immunoglobulin-type amyloid. The results also demonstrate here an increase in hydrophobicity during amyloidogenesis of immunoglobulin-derived amyloid fibril proteins, here.
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Max-Planck-Institut für Biochemie, Martinsried bei München.
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D001536:Bence Jones Protein / Q000737:chemistry* / Q000652:urine; D004586:Electrophoresis; D006801:Humans; D006868:Hydrolysis; D007074:Immunoglobulin G / Q000276:immunology
D007074:Immunoglobulin G; D001536:Bence Jones Protein