Scrapie-associated fibrils (SAF) purification method yields amyloid proteins from systemic and cerebral amyloidosis
- 1 May 1986
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 6 (5) , 459-465
- https://doi.org/10.1007/bf01116137
Abstract
We identified fibrils from non-transmissible systemic and cerebral amyloidosis using the purification method of scrapie-associated fibrils (SAF). The fibrils possessed the same nature of congophilia, filamentous structures and molecular weights as amyloid fibrils, and were resistant to Proteinase K digestion. This SAF method makes for a rapid extraction from amyloid-laden tissues. The method, therefore, may purify nontransmissible amyloids alone or together with SAF proteins.This publication has 18 references indexed in Scilit:
- Infection-Specific Particle from the Unconventional Slow Virus DiseasesScience, 1984
- A rapid and efficient method to enrich SAF-protein from scrapie brains of hamstersBioscience Reports, 1984
- Scrapie infectivity, fibrils and low molecular weight proteinNature, 1983
- Scrapie-associated fibrils in Creutzfeldt–Jakob diseaseNature, 1983
- Towards Purification of the Scrapie AgentEuropean Journal of Biochemistry, 1983
- Abnormal fibrils from scrapie-infected brainActa Neuropathologica, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The characterization of soluble amyloid prepared in waterJournal of Clinical Investigation, 1968
- HIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF THE AMYLOID FIBRILThe Journal of cell biology, 1967
- THE ISOLATION OF AMYLOID FIBRILS AND A STUDY OF THE EFFECT OF COLLAGENASE AND HYALURONIDASEThe Journal of cell biology, 1964