Abstract
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 language | English |
|---|---|
| Pages (from-to) | 227-231 |
| Number of pages | 5 |
| Journal | Gastroenterologia Japonica |
| Volume | 19 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jun 1984 |
| Externally published | Yes |
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Keywords
- γ-GTP
- Pancreatic cancer
- Pancreatic cancer cell line
ASJC Scopus subject areas
- Gastroenterology
Cite this
Characterization of γ-gtp in a human pancreatic cancer cell line. / Sugimoto, Manabu; Yamaguchi, Nozomi; Kawai, Keiichi.
In: Gastroenterologia Japonica, Vol. 19, No. 3, 06.1984, p. 227-231.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of γ-gtp in a human pancreatic cancer cell line
AU - Sugimoto, Manabu
AU - Yamaguchi, Nozomi
AU - Kawai, Keiichi
PY - 1984/6
Y1 - 1984/6
N2 - 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.
AB - 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.
KW - γ-GTP
KW - Pancreatic cancer
KW - Pancreatic cancer cell line
UR - http://www.scopus.com/inward/record.url?scp=0021270059&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021270059&partnerID=8YFLogxK
U2 - 10.1007/BF02779174
DO - 10.1007/BF02779174
M3 - Article
VL - 19
SP - 227
EP - 231
JO - Journal of Gastroenterology
JF - Journal of Gastroenterology
SN - 0944-1174
IS - 3
ER -