Amino acid sequence analyses of non-AA proteins from amyloid fibrils of bovine kidney.
The elution pattern obtained when amyloid fibrils from amyloid-laden bovine kidneys were subjected to gel filtration under dissociating conditions revealed a larger amount of non-AA material (eluting between the void volume and protein AA) than usually seen in other species. SDS-PAGE of this non-AA fraction yielded several Coomassie blue stained bands. The most distinctive ones gave estimated molecular masses of 15 kDa, 18 kDa, 33 kDa and 43 kDa. These molecular species were electroblotted onto PVDF membranes, and were further characterized by amino acid composition analyses, cyanogen bromide cleavage and N-terminal analyses. The results revealed that the intermediate 'non-AA' fraction consisted of histones H2B, H3 and H4 in addition to protein AA also found in this fraction.
Veiby
O P
OP
Department of Biochemistry, University of Oslo, Norway.
Sletten
K
K
Husby
G
G
Nordstoga
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D007668:Kidney / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D000685:Serum Amyloid A Protein / Q000737:chemistry* / Q000302:isolation & purification
D000596:Amino Acids; D008565:Membrane Proteins; D000685:Serum Amyloid A Protein; D003488:Cyanogen Bromide