Micropurification techniques in the analysis of amyloid proteins
- Correspondence to: Dr B Kaplan, Heller Institute of Medical Research, Sheba Medical Centre, Tel Hashomer 52621, Israel; roman{at}taro.co.il
- Accepted 13 September 2002
Abstract
This review describes the different microtechniques developed for the extraction and purification of amyloid proteins from small specimens of fresh and formalin fixed tissues. These procedures differ with respect to solvent type, extraction conditions, and protein purification strategy. The advantages and disadvantages of the different microtechniques are discussed by taking into consideration tissue type (fresh of fixed) and size, amyloid type, and its content in the tissue. The review demonstrates the applicability of these techniques for the immunochemical and chemical characterisation of amyloid in different clinical forms of amyloidosis and in experimental small animal models. The clinical value of the applied microtechniques and their importance in the study of the pathogenesis of amyloid related diseases are outlined.
- AA, amyloid protein A
- Aβ, amyloid β protein or peptide
- AβPP, amyloid β protein precursor
- AD, Alzheimer’s disease
- AL, amyloid immunoglobulin light chains
- apo, apoliprotein
- ATTR, amyloid transthyretin
- HPLC, high performance liquid chromatography
- PVDF, polyvinyl difluoride
- SAA, serum amyloid A protein
- SDS, sodium dodecyl sulfate
- SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis
- TFA, trifluoroacetic acid
- TTR, transthyretin
