Isolation and sequencing of a new biologically active peptide from human lung carcinoma.
A biologically active peptide designated hLCP has been isolated and purified to homogeneity from human lung carcinoma by means of acidic extraction and successive chromatography on Sephadex G-50, Toyopearl HW-40 F and reverse-phase high performance liquid chromatography columns. Analysis showed that peptide consists of thirteen amino acids. Primary structure of hLCP has been deduced by double-coupling Edman degradation combined with enzyme digestion as H-Ser-Pro-Pro-Asp-Gly-Lys-Lys-Glx-Ser-Ala-Asp-Val-Lys-OH. hLCP possessed significant excitatory activity on an electrical stimulation induced contraction. No hLCP could be detected in normal lung tissue. The possibility of using hLCP as a biochemical marker in the clinic for the early detection of lung carcinoma is being investigated.
D000368:Aged; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002294:Carcinoma, Squamous Cell / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008175:Lung Neoplasms / Q000032:analysis*; D008297:Male; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000032:analysis* / Q000302:isolation & purification; D010455:Peptides / Q000032:analysis* / Q000302:isolation & purification
D000596:Amino Acids; D009363:Neoplasm Proteins; D010455:Peptides