Characterization of γ-gtp in a human pancreatic cancer cell line

Manabu Sugimoto, Nozomi Yamaguchi, Keiichi Kawai

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Gamma-glutamyl transpeptidase (γ-GTP) was partially purified from human normal pancreas, pancreatic carcinoma and a human pancreatic cancer cell line, HPC-Y1. The characteristics of γ-GTP from all three samples appeared to be identical. The estimated molecular weight of samples solubilized with Triton X-100 was 210K and that of bromelain-solubilized γ-GTP was 110K. On polyacrylamide gel electrophoresis, the main band in both the Triton- and the bromelain-solubilized γ-GTP of these samples had similar electrophoretic mobility. The percentages binding with concanavalin A were 52%-62%, while on isoelectric focusing the pI values were 3.40-3.45. It was concluded that the heterogeneity of the γ-GTP isoenzyme could not be identified by either gel filtration or polyacrylamide gel electrophoresis, and it is necessary to investigate the modification of carbohydrate structure on tumor.

Original languageEnglish
Pages (from-to)227-231
Number of pages5
JournalGastroenterologia Japonica
Issue number3
Publication statusPublished - Jun 1 1984
Externally publishedYes


  • Pancreatic cancer
  • Pancreatic cancer cell line
  • γ-GTP

ASJC Scopus subject areas

  • Gastroenterology


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