The Influence of Both Urea and 2,2,2-Trifluoroethanol in the Amyloid Fibril Formation of Bovine Serum Albumin

A profound conformational conversion coupled with the temporal evolution of morphologically-distinct ring-like nanoscopic intermediates were monitored during the amyloid assembly of human serum albumin into β-sheet-rich fibrils.

Download Full-text

Insights into the Mechanism of Aggregation and Fibril Formation from Bovine Serum Albumin

The Journal of Physical Chemistry B ◽

10.1021/jp111528c ◽

2011 ◽

Vol 115 (14) ◽

pp. 4195-4205 ◽

Cited By ~ 119

Author(s):

Mily Bhattacharya ◽

Neha Jain ◽

Samrat Mukhopadhyay

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Fibril Formation

Download Full-text

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100079632 ◽

1977 ◽

Vol 35 ◽

pp. 438-439

Author(s):

T. Shirahama ◽

M. Skinner ◽

A.S. Cohen

Keyword(s):

Amyloid Fibril ◽

Close Association ◽

Gel Filtration ◽

Fibril Formation ◽

Amyloid Protein ◽

Electron Microscopic ◽

Amyloid Deposits ◽

Amyloid Fibril Formation ◽

Electron Microscopic Technique ◽

Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

Download Full-text

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

1987 ◽

Vol 45 ◽

pp. 762-763

Author(s):

G. D. Gagne ◽

M. F. Miller

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Artificial Substrate ◽

Chemical Fixation ◽

As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Download Full-text