Analysis of amyloid fibrils in the cheetah (Acinonyx jubatus)
Recently, a high prevalence of amyloid A (AA) amyloidosis has been documented among captive cheetahs worldwide. Biochemical analysis of amyloid fibrils extracted from the liver of a Japanese captive cheetah unequivocally showed that protein AA was the main fibril constituent. Further characterizatio...
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Published in | Amyloid Vol. 13; no. 2; pp. 93 - 98 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Informa UK Ltd
01.06.2006
Taylor & Francis Taylor & Francis Ltd |
Subjects | |
Online Access | Get full text |
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Summary: | Recently, a high prevalence of amyloid A (AA) amyloidosis has been documented among captive cheetahs worldwide. Biochemical analysis of amyloid fibrils extracted from the liver of a Japanese captive cheetah unequivocally showed that protein AA was the main fibril constituent. Further characterization of the AA fibril components by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis revealed three main protein AA bands with approximate molecular weights of 8, 10 and 12 kDa. Mass spectrometry analysis of the 12-kDa component observed in SDS-PAGE and Western blotting confirmed the molecular weight of a 12,381-Da peak. Our finding of a 12-kDa protein AA component provides evidence that the cheetah SAA sequence is longer than the previously reported 90 amino acid residues (∼10 kDa), and hence SAA is part of the amyloid fibril. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1350-6129 1744-2818 |
DOI: | 10.1080/13506120600722621 |