Primary structure of human lymphotoxin derived from 1788 lymphoblastoid cell line.
The amino acid sequence of human lymphotoxin derived from a 1788 lymphoblastoid cell line was determined. Peptide fragments obtained by trypsin, lysine-C peptidase, cyanogen bromide, and acetic acid cleavage of the intact protein were purified by reverse-phase high performance liquid chromatography and analyzed by amino acid composition and by automated Edman degradation. The protein is 171 amino acids long with a molecular weight of 18,664. It contains one asparagine-linked glycosylation site and lacks cysteine. The salient features of the amino acid sequence of lymphotoxin are described.
D000085:Acetates; D019342:Acetic Acid; D000595:Amino Acid Sequence; D002268:Carboxypeptidases; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D010450:Endopeptidases; D006801:Humans; D008214:Lymphocytes / Q000032:analysis*; D008233:Lymphotoxin-alpha; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D000085:Acetates; D008233:Lymphotoxin-alpha; D010446:Peptide Fragments; C025427:carboxypeptidase P; D002268:Carboxypeptidases; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; C044574:lysine-C peptidase; D003488:Cyanogen Bromide; D019342:Acetic Acid