Isolation and sequencing of a new biologically active peptide from human lung carcinoma.

Abstract

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.

• Authors: K L Hsi, S X Wu, Z G Chen, X Y Guo, K Tsou
• Journal: Biomedical chromatography : BMC (Biomed Chromatogr) Vol. 1 Issue 3 Pg. 119-22 (Jun 1986) ISSN: 0269-3879 [Print] England
• PMID: 3506821 (Publication Type: Journal Article)

Chemical References

• Amino Acids
• Neoplasm Proteins
• Peptides

Topics

• Aged
• Amino Acid Sequence
• Amino Acids (analysis)
• Carcinoma, Squamous Cell (analysis)
• Chromatography, High Pressure Liquid
• Humans
• Lung Neoplasms (analysis)
• Male
• Molecular Sequence Data
• Neoplasm Proteins (analysis, isolation & purification)
• Peptides (analysis, isolation & purification)