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Alkali‐Degradation of Amyloid: An Ancient Method Useful for Making Monoclonal Antibodies Against Amyloid Fibril Proteins
Author(s) -
Westermark G. T.,
Sletten K.,
Westermark P.
Publication year - 2009
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.1365-3083.2009.02336.x
Subject(s) - monoclonal antibody , amyloid (mycology) , fibril , amyloid fibril , antibody , chemistry , immunohistochemistry , polymerization , pathology , biochemistry , biology , amyloid β , medicine , disease , immunology , polymer , inorganic chemistry , organic chemistry
The systemic amyloidoses constitute a group of life‐threatening disorders at which one out of about 15 different proteins have polymerized into fibrils. Prognosis and treatment varies widely and depends on the biochemical type. Determination of this has usually to be performed by immunohistochemistry which is a challenge because of lack of monospecific antibodies that can be used on formaldehyde‐fixed tissue sections. We have here used an old method to create immunogenic fragments of AL‐amyloid fibrils by partial degradation and solubilization with sodium hydroxide. The mouse monoclonal antibody pwlam raised against this material, labelled AL‐amyloid deposits of lambda origin strongly and specifically in sections of formaldehyde‐fixed and paraffin‐embedded tissues.