ABSTRACT
This chapter analyzes the precursor protein of the amyloidosis in 5 frozen kidney samples of the bovines and clarifies the characterization of bovine amyloidosis. Amyloid fibrils were extracted from 10g frozen kidney samples using a modified water extraction method. Thereafter, SDS-PAGE, immunoblotting, and matrix-assisted laser desorption ionization/time-of-flight mass spectrometry were perofrmed for detecting the amyloid precursor proteins. Diffuse congophilic amorphous substances were found predominantly in the glomerulus of all the 5 bovine kidney samples. By immunohistochemistry, positive reaction for the rabbit anti-human AA serum and the sheep anti-human Serum amyloid A antibody was observed in the lesions where Congo red staining was positive. SDS-PAGE revealed that fibril proteins were visualized as two major bands of about 10 kDa and about 14 kDa in addition to a few minor bands.
