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• W2023444769 abstract "Motivated by the finding that the amino acid sequence of the Bence Jones protein BJP-DIA was identical to that of the main protein component of the amyloid fibrils obtained from the same patient with AL-amyloidosis, (Klafki, H.-W., Kratzin, H.-D., Pick, A.-I., Eckart, K., Karas, M. & Hilschmann, N. (1992) Biochemistry 31, 3265-3272.), we attempted to create amyloid-like fibrils from the Bence Jones protein in vitro, without addition of proteolytic enzymes. Reduction of BJP-DIA, solubilized in PBS, pH 7.4, overnight at 37 degrees C resulted in the formation of a precipitate which had affinity for the dye Congo red. Electron microscopy of negatively stained samples of the reduced protein revealed aggregates of linear unbranched fibrils. SDS-polyacrylamide gel electrophoresis demonstrated that the precipitate consisted almost exclusively of intact light chain molecules. This result makes it possible to deduce a molecular model of these amyloid fibrils generated in vitro." @default.
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• W2023444769 date "1993-01-01" @default.
• W2023444769 modified "2023-09-26" @default.
• W2023444769 title "Reduction of Disulfide Bonds in an Amyloidogenic Bence Jones Protein Leads to Formation of “Amyloid-Like” Fibrils in Vitro" @default.
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• W2023444769 doi "https://doi.org/10.1515/bchm3.1993.374.7-12.1117" @default.
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