The Amino-Acid Sequence of the Variable Region of a Carbohydrate-Containing Amyloid Fibril Protein EPS (Immunoglobulin Light Chain, Type λ)

1985 ◽  
Vol 366 (2) ◽  
pp. 617-626 ◽  
Author(s):  
Kim G. TOFT ◽  
Knut SLETTEN ◽  
Gunnar HUSBY
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Immunoglobulin Light Chain ◽  
Light Chain Type ◽  
Amyloid Fibril Protein ◽  
Chain Type

scholarly journals The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein AR

1981 ◽  
Vol 195 (3) ◽  
pp. 561-572 ◽  
Author(s):  
K Sletten ◽  
J B Natvig ◽  
G Husby ◽  
J Juul
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Amino Acid Residues ◽  
Variable Regions ◽  
Light Chain Type ◽  
Amyloid Fibril Protein ◽  
Chain Type

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].

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

1986 ◽  
Vol 239 (3) ◽  
pp. 545-551 ◽  
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.

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

1985 ◽  
Vol 232 (1) ◽  
pp. 183-190 ◽  
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.

scholarly journals The primary structure of the variable region of an immunoglobin IV light-chain amyloid-fibril protein (AL GIL)

1988 ◽  
Vol 256 (3) ◽  
pp. 973-980 ◽  
Author(s):  
E M Fykse ◽  
K Sletten ◽  
G Husby ◽  
G G Cornwell
Keyword(s):  
Amino Acid ◽  
Light Chain ◽  
Primary Structure ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Acceptor Site ◽  
Amino Acid Residues ◽  
Bence Jones Protein ◽  
Sequence Homologies ◽  
Amyloid Fibril Protein

The primary structure of the variable region of an amyloid-fibril protein GIL of immunoglobulin lambda-light-chain origin (AL) was determined. The AL protein obtained from the fibrils in the spleen of a 54-year-old man with primary systemic amyloidosis could be assigned to subgroup IV of the lambda variable-region sequence. About 50% of the protein was found to be truncated in the N-terminus and lacked the first six amino acid residues. The polypeptides consisted of about 146 amino acid residues and contained traces of carbohydrate. An acceptor site for N-glycosylation was found in positions 90-93, but no glycopeptide could be isolated. Comparison of the amino acid sequence of AL protein GIL with that of the only Bence-Jones protein of subgroup IV previously studied revealed a sequence homology of 89%. A similar comparison made with other AL proteins gave sequence homologies below 66%.

scholarly journals NEW, THIRD CLASS OF AMYLOID FIBRIL PROTEIN

1974 ◽  
Vol 139 (3) ◽  
pp. 773-778 ◽  
Author(s):  
G. Husby ◽  
J. B. Natvig ◽  
K. Sletten
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Primary Amyloidosis ◽  
Amyloid Proteins ◽  
Immunoglobulin Light Chain ◽  
Structural Identity ◽  
Amyloid Fibril Protein

An unusual protein AR was isolated from the amyloid fibril preparation derived from a patient with primary amyloidosis. Protein AR was unique in its antigenicity, and revealed no structural identity with any known amyloid proteins or with immunoglobulin chains or fragments. Thus a new third class of amyloid fibril proteins besides the immunoglobulin light-chain variable region fragments and the nonimmunoglobulin protein AS, has been characterized. A component antigenically related to protein AR was found in the serum of the patient.

Immunoglobulin light-chain type in Sjögren's syndrome

1983 ◽  
Vol 14 (4) ◽  
pp. 380
Author(s):  
Guillermo J. Ruiz-Argüelles ◽  
Efraín Díaz-Jouanen ◽  
Donato Alarcó-Segovia
Keyword(s):  
Sjögren’S Syndrome ◽  
Light Chain ◽  
Sjögren's Syndrome ◽  
Sjogren’S Syndrome ◽  
Sjogren's Syndrome ◽  
Immunoglobulin Light Chain ◽  
Light Chain Type ◽  
Chain Type ◽  
Sjögren‘S Syndrome
Sign in / Sign up

Export Citation Format

Share Document