The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils

Insights

Researchers determined the amino acid sequence of the acid-soluble fraction (ASF) protein in amyloid fibrils from familial Mediterranean fever patients. This protein, lacking cysteine, differs from immunoglobulins and is not found in myeloma-associated amyloid.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Amyloid fibrils are associated with various diseases, including familial Mediterranean fever and secondary amyloidosis.
  • The composition of amyloid fibrils is not fully understood, particularly the role of specific protein components.

Purpose of the Study:

  • To determine the complete amino acid sequence of the acid-soluble fraction (ASF) protein found in amyloid fibrils.
  • To compare the ASF protein sequence with proteins from other amyloidosis types.

Main Methods:

  • Amino acid sequencing of the purified acid-soluble fraction (ASF) from amyloid fibrils.
  • Partial amino acid sequencing of proteins from secondary amyloidosis patients.

Main Results:

  • The complete amino acid sequence of the ASF protein was obtained.
  • ASF contains no cysteine and differs from known immunoglobulins.
  • Partial sequences of proteins from secondary amyloidosis were largely identical to ASF, with one exception (alanine-valine interchange).
  • ASF was not detected in myeloma-associated amyloid.

Conclusions:

  • The acid-soluble fraction (ASF) is a distinct protein component of amyloid fibrils in familial Mediterranean fever.
  • ASF's unique sequence suggests a specific role in amyloid formation.
  • Further research is needed to elucidate ASF's function and its relationship to other amyloid proteins.

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