BIOMAT Database Logo BIOMAT Database Logo

Structural studies of a carbohydrate-containing immunoglobulin-lambda-light-chain amyloid-fibril protein (AL) of variable subgroup III. 1986

E Holm, and K Sletten, and G Husby

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.

UI MeSH Term Description Entries
D007142 Immunoglobulin gamma-Chains Heavy chains of IMMUNOGLOBULIN G having a molecular weight of approximately 51 kDa. They contain about 450 amino acid residues arranged in four domains and an oligosaccharide component covalently bound to the Fc fragment constant region. The gamma heavy chain subclasses (for example, gamma 1, gamma 2a, and gamma 2b) of the IMMUNOGLOBULIN G isotype subclasses (IgG1, IgG2A, and IgG2B) resemble each other more closely than the heavy chains of the other IMMUNOGLOBULIN ISOTYPES. Immunoglobulins, gamma-Chain,Immunoglobulin gamma-Chain,gamma Immunoglobulin Heavy Chain,gamma Immunoglobulin Heavy Chains,gamma-1-Immunoglobulin Heavy Chain,gamma-2a-Immunoglobulin Heavy Chain,gamma-2b-Immunoglobulin Heavy Chain,gamma-Chain Immunoglobulins,Heavy Chain, gamma-1-Immunoglobulin,Heavy Chain, gamma-2a-Immunoglobulin,Heavy Chain, gamma-2b-Immunoglobulin,Immunoglobulin gamma Chain,Immunoglobulin gamma Chains,Immunoglobulins, gamma Chain,gamma 1 Immunoglobulin Heavy Chain,gamma 2a Immunoglobulin Heavy Chain,gamma 2b Immunoglobulin Heavy Chain,gamma Chain Immunoglobulins,gamma-Chain, Immunoglobulin,gamma-Chains, Immunoglobulin
D007143 Immunoglobulin Heavy Chains The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa. Immunoglobulins, Heavy-Chain,Heavy-Chain Immunoglobulins,Ig Heavy Chains,Immunoglobulin Heavy Chain,Immunoglobulin Heavy Chain Subgroup VH-I,Immunoglobulin Heavy Chain Subgroup VH-III,Heavy Chain Immunoglobulins,Heavy Chain, Immunoglobulin,Heavy Chains, Ig,Heavy Chains, Immunoglobulin,Immunoglobulin Heavy Chain Subgroup VH I,Immunoglobulin Heavy Chain Subgroup VH III,Immunoglobulins, Heavy Chain
D007147 Immunoglobulin Light Chains Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule. Ig Light Chains,Immunoglobulins, Light-Chain,Immunoglobulin Light Chain,Immunoglobulin Light-Chain,Light-Chain Immunoglobulins,Chains, Ig Light,Chains, Immunoglobulin Light,Immunoglobulins, Light Chain,Light Chain Immunoglobulins,Light Chain, Immunoglobulin,Light Chains, Ig,Light Chains, Immunoglobulin,Light-Chain, Immunoglobulin
D008297 Male Males
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D002241 Carbohydrates A class of organic compounds composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n. The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrate
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000368 Aged A person 65 years of age or older. For a person older than 79 years, AGED, 80 AND OVER is available. Elderly
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid

Related Publications

E Holm, and K Sletten, and G Husby
The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS (immunoglobulin light chain, type lambda).
July 1985, Biological chemistry Hoppe-Seyler,
E Holm, and K Sletten, and G Husby
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).
September 1990, The Journal of investigative dermatology,
E Holm, and K Sletten, and G Husby
The amino acid sequence of a carbohydrate-containing immunoglobulin-light-chain-type amyloid-fibril protein.
November 1985, The Biochemical journal,
E Holm, and K Sletten, and G Husby
Characterization of an amyloid fibril protein from localized amyloidosis of the skin as lambda immunoglobulin light chains of variable subgroup I (A lambda I).
July 1981, Clinical and experimental immunology,
E Holm, and K Sletten, and G Husby
Primary structure of a deleted human lambda type immunoglobulin light chain containing carbohydrate: protein Sm lambda.
November 1975, Proceedings of the National Academy of Sciences of the United States of America,
E Holm, and K Sletten, and G Husby
The precursor molecule of a V lambda II-immunoglobulin light chain-derived amyloid fibril protein circulates precleaved.
August 1993, Biochemical and biophysical research communications,
E Holm, and K Sletten, and G Husby
The complete amino acid sequence of a prototype immunoglobulin-lambda light-chain-type amyloid-fibril protein AR.
June 1981, The Biochemical journal,
E Holm, and K Sletten, and G Husby
Amyloid fibril protein related to immunoglobulin lambda-chains.
April 1975, Journal of immunology (Baltimore, Md. : 1950),
E Holm, and K Sletten, and G Husby
N-terminal amino acid sequence of amyloid fibril protein AR, prototype of a new lambda-variable subgroup, V lambda V.
January 1974, Scandinavian journal of immunology,
E Holm, and K Sletten, and G Husby
Constant region of a kappa III immunoglobulin light chain as a major AL-amyloid protein.
July 1998, Scandinavian journal of immunology,
Copied contents to your clipboard!