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Isolation and sequencing of a new biologically active peptide from human lung carcinoma
Author(s) -
Hsi Kuoling,
Wu Shihxiang,
Chen Zhongguang,
Guo Xiuyue,
Tsou Kang
Publication year - 1986
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130010306
Subject(s) - edman degradation , chemistry , peptide , chromatography , sephadex , carcinoma , human lung , biological activity , amino acid , lung , enzyme , biochemistry , peptide sequence , medicine , gene , in vitro
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 possesed 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.