[Rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), II: isolation and amino acid sequence of the tyrptic peptides from the H-chain (author's transl)].
The reduced and carboxymethylated H-chain of protein Nie was digested with trypsin. 40 tryptic peptides were isolated from the digest by ion exchange chromatography, accounting for the entire amino acid composition of the polypeptide chain. Sequence studies performed with these fragments revealed the position of 444 out of 448 residues. In addition 8 overlapping cleavage products were purified which contributed to the ordering of tryptic peptides in the chain.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D006801:Humans; D007074:Immunoglobulin G / Q000032:analysis*; D007143:Immunoglobulin Heavy Chains / Q000032:analysis*; D009194:Myeloma Proteins / Q000032:analysis*; D010084:Oxidation-Reduction; D014357:Trypsin
D000596:Amino Acids; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D009194:Myeloma Proteins; D014357:Trypsin
Zur Strukturregel der Antikörper. Die Primärstruktur eines monoklonalen IgG1-Immunoglobulins (Myelomprotein Nie), II. [1,2] Isolierung und Aminosäuresequenz der tryptischen Peptide der H-Kette