Partial amino acid sequence of an amyloid fibril protein from nodular primary cutaneous amyloidosis showing homology to lambda immunoglobulin light chain of variable subgroup III (a lambda III).

Abstract

An amyloid fibril protein (MA) was purified as a 17,000-dalton protein from a case of nodular primary cutaneous amyloidosis, and its partial amino acid sequence (22 residues from N-terminal) was determined. A sequence closely homologous to that of the lambda III subgroup of the immunoglobulin light chain was detected. This is the third case of nodular primary cutaneous amyloidosis which has been studied at the level of sequence analysis of purified amyloid fibril proteins, and the first case of nodular primary cutaneous amyloidosis in which a lambda III amyloid protein has been shown to be present by sequence analysis.

• Authors: Y Kitajima, H Hirata, Y Kagawa, H Yaoita
• Journal: The Journal of investigative dermatology (J Invest Dermatol) Vol. 95 Issue 3 Pg. 301-3 (Sep 1990) ISSN: 0022-202X [Print] United States
• PMID: 2117035 (Publication Type: Journal Article)

Chemical References

• Amino Acids
• Amyloid
• Immunoglobulin Light Chains

Topics

• Amino Acid Sequence
• Amino Acids (analysis)
• Amyloid (analysis)
• Amyloidosis (metabolism)
• Female
• Humans
• Immunoglobulin Light Chains (genetics)
• Middle Aged
• Molecular Sequence Data
• Sequence Homology, Nucleic Acid
• Skin Diseases (metabolism)