[The primary structure of crystallizable monoclonal immunoglobulin IgG1 Kol. II. Amino acid sequence of the L-chain, gamma-type, subgroup I].
The immunoglobulin Kol was the first intact antibody molecule which was characterized by high-resolution X-ray crystallography. Furthermore the complete amino-acid sequence of the heavy (H)-chain is known. Here we report the complete amino-acid sequence of the light (L)-chain of the monoclonal immunoglobulin Kol (IgG1). The polypeptide has an Mr of 22,781, consists of 216 amino acids and due to its structure is of the lambda-type. With the characteristic amino acids threonine, asparagine, threonine, glycine and lysine in positions 101, 114, 116, 154, and 165, respectively the Kol L-chain is of the Mcg isotype. With the proteins Mcg, Mot, Bur, Loc and Mem six myeloma-derived amino-acid sequences of the same isotype are known. The amino-acid sequence of the N-terminal variable part is characteristic of subgroup 1. This contribution completes the primary structure of IgG1 Kol.
Kratzin
H D
HD
max-Planck-Institut für experimentelle Medizin, Abteilung Immunchemie, Göttingen.
Palm
W
W
Stangel
M
M
Schmidt
W E
WE
Friedrich
J
J
Hilschmann
N
N
D000478:Alkylation; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal / Q000032:analysis; D003460:Crystallization; D006868:Hydrolysis; D007074:Immunoglobulin G / Q000032:analysis*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D014961:X-Ray Diffraction
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D007074:Immunoglobulin G
Die Primärstruktur des kristallisierbaren monoklonalen Immunglobulins IgG1 Kol. II. Aminosäuresequenz der L-Kette, lambda-Typ, Subgruppe I.