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Amino Acid Sequence Analyses of Non‐AA Proteins from Amyloid Fibrils of Bovine Kidney
Author(s) -
VEIBY O. P.,
SLETTEN K.,
HUSBY G.,
NORDSTOGA K.
Publication year - 1992
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1992.tb02834.x
Subject(s) - cyanogen bromide , chemistry , size exclusion chromatography , amino acid , coomassie brilliant blue , peptide sequence , cleavage (geology) , biochemistry , fibril , amyloid (mycology) , chromatography , microbiology and biotechnology , staining , biology , enzyme , paleontology , inorganic chemistry , genetics , fracture (geology) , gene
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 PAOF, 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 PVDK membranes, and wore 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.