Premium
A Second Component in Bovine AA Amyloid Fibrils Not Identical with Protein AA Is Essential for AA Amyloid Fibrillogenesis
Author(s) -
HOL P. R.,
LANGE VELD J.P.M.,
BEUNINGENJANSEN E. W.,
VEERKAMP J. H.,
GRUYS E.
Publication year - 1984
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.1365-3083.1984.tb00977.x
Subject(s) - chemistry , fibril , fibrillogenesis , amyloid (mycology) , guanidine , congo red , amyloidosis , amyloid fibril , size exclusion chromatography , biochemistry , chromatography , amyloid β , enzyme , organic chemistry , medicine , inorganic chemistry , disease , adsorption , pathology
Amyloid fibrils were isolated from the renal papillae and glomeruli of cows with spontaneous AA amyloidosis. The fibrils were solubilized by treatment with guanidine hydrochloride (Gu HCl) and subjected to gel filtration on Sephacryl S‐200. Two other fractions were obtained beside the void volume and the AA fractions. Reaggregation studies were performed by dialysing the fractions, separately or in combinations, against Gu‐HCl‐free solutions. Protein AA alone (about 10 kd) appeared not to precipitate. The olher fractions alone and the combinations of fractions tested formed precipitates. The precipitates containing all fractions (including prolein AA) or protein AA plus a fraction containing a 14‐ and a 23‐kd protein revealed congophilic green birefringent fibrillar material. Dialysis against acidic and calcium‐containing solutions gave the best results. Amyloid fibril‐like material was visible on electron microscopic examination. The amino acid composition of the 19 + 23‐kd material appeared to be slightly different from protein A A and evidently unlike SAP. On imniunolluorescence‐absorbance studies the 19 + 23‐kd material appeared evidently unlike protein A A and SAP. From these findings it is concluded that for spontaneous formation of A A amyloid fibrils other non‐AA proteins are necessary.