Partial Amino Acid Sequence of an Amyloid Fibril Protein from Nodular Primary Cutaneous Amyloidosis Showing Homology to λ Immunoglobulin Light Chain of Variable Subgroup III (A λ III)

The amino acid sequence of an amyloid-fibril protein of immunoglobulin light-chain type (AL) was elucidated. The sequence determination involved digesting the protein with trypsin, thermolysin and pepsin. The protein was found to consist of 154 amino acid residues and is thus missing about half of the constant region of a light chain. A certain heterogeneity in the length of the polypeptide was observed in the C-terminal region. The amino acid sequence from CDR (complementary-determining region) 1 and FR (framework region) 3 indicated an oligoclonal origin of the protein. By comparing the primary structure of protein AR with other lambda- and even kappa-chains, it was revealed that protein AR had an insertion of two residues of aspartic acid, namely residues 68 and 69, which has not been reported previously in light chains. The overall sequence homology in the variable region showed that protein AR is more similar to V lambda V than to the other subgroups [Kabat, Wu & Bilofsky (1979) Variable regions of Immunoglobulin Chains, Medical Computer Systems, Bolt, Beranek and Newman, Cambridge, MA].

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The amino acid sequence of a carbohydrate-containing immunoglobulin-light-chain-type amyloid-fibril protein

Biochemical Journal ◽

10.1042/bj2320183 ◽

1985 ◽

Vol 232 (1) ◽

pp. 183-190 ◽

Cited By ~ 26

Author(s):

T Tveteraas ◽

K Sletten ◽

P Westermark

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Light Chain ◽

Amyloid Fibrils ◽

Amyloid Fibril ◽

Amino Acid Residues ◽

Hypervariable Regions ◽

Glycosylation Sites ◽

Amyloid Fibril Protein ◽

Chain Type

The amino acid sequence of an amyloid-fibril protein Es492 of immunoglobulin-lambda-light-chain origin (AL) was elucidated. The amyloid fibrils were obtained from the spleen of a patient who died from systemic amyloidosis. The amino acid sequence was elucidated from structural studies of peptides derived from digestion of the protein with trypsin, thermolysin, chymotrypsin and Staphylococcus aureus V8 proteinase and from cleavage of the protein with CNBr and BNPS-skatole. A heterogeneity in the length of the polypeptide was seen in the C-terminal region. The protein was by sequence homology to other lambda-chains shown to be of the V lambda II subgroup. Although an extensive homology was seen, some amino acid residues in positions 26, 31, 32, 40, 44, 93, 97, 98 and 99 have not previously been reported in these positions of V lambda II proteins. The significance of these residues in the fibril formation is unclear. The protein was found to contain carbohydrate, with glycosylation sites in two of the hypervariable regions.

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An amyloid fibril protein of unknown origin: Partial amino-acid sequence analysis

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(72)80166-9 ◽

1972 ◽

Vol 46 (2) ◽

pp. 498-500 ◽

Cited By ~ 34

Author(s):

D. Ein ◽

S. Kimura ◽

G.G. Glenner

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Amyloid Fibril ◽

Unknown Origin ◽

Amino Acid Sequence Analysis ◽

Partial Amino Acid Sequence ◽

Amyloid Fibril Protein

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Structural studies of a carbohydrate-containing immunoglobulin-λ-light-chain amyloid-fibril protein (AL) of variable subgroup III

Biochemical Journal ◽

10.1042/bj2390545 ◽

1986 ◽

Vol 239 (3) ◽

pp. 545-551 ◽

Cited By ~ 15

Author(s):

E Holm ◽

K Sletten ◽

G Husby

Keyword(s):

Amino Acid ◽

Light Chain ◽

Amyloid Fibril ◽

Gel Filtration ◽

Hypervariable Region ◽

Variable Region ◽

Amino Acid Residues ◽

Immunoglobulin Light Chain ◽

Amyloid Fibril Protein ◽

Chain Type

The amino acid sequence of the variable region of a carbohydrate-containing amyloid-fibril protein MOL of immunoglobulin-light-chain type (AL) was elucidated. The sequence determination involved cleaving the protein with CNBr, BNPS-skatole, thermolysin and trypsin. The sequenced protein consisted of about 130 amino acid residues; however, gel-filtration and N-terminal analysis studies revealed AL proteins ranging in Mr from about 10,000 to 25,000. The oligosaccharide chain was found to be bound in the hypervariable region. By sequence homology to other lambda chains the AL protein MOL was shown to be of the V lambda III subgroup.

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