Further characterization of bombesin like immunoreactivities from the skin of Korean fire-bellied toad, Bombina orientalis.
- Author:
Hyeok Yil KWON
1
;
Hyung Seo PARK
;
Moo Ho WON
;
Yun Lyul LEE
;
Jin Hyoung PARK
Author Information
1. Department of Physiology College of Medicine, Hallym University, Chunchon, Kangwon-Do 200-702, Korea.
- Publication Type:Original Article
- Keywords:
Bombesin;
Bombesin like immunoreactivity;
Frog skin peptide;
Molecular;
heterogeneity;
Gastric release;
Pancreatic exocrine secretion obligation
- MeSH:
Anura*;
Bombesin*;
Chromatography;
Chromatography, High Pressure Liquid;
Population Characteristics;
Skin*
- From:The Korean Journal of Physiology and Pharmacology
1998;2(5):637-644
- CountryRepublic of Korea
- Language:English
-
Abstract:
Previously, we have isolated authentic bombesin and another bombesin like peptide named bombesin like immunoreactivity (BLI)-K2 from the skin of Korean fire-bellied toad, Bombina orientalis. In the present study, we have newly purified three heterogeneous forms of BLI named BLI-K3, BLI-K4, and BLI-K5 from side fractions obtained in previous isolation of bombesin like peptide. The BLIs were separated into five peaks on a column of C18 preparative HPLC. Among them, three minor peaks containing BLI-K3, K4, and K5 were purified by means of sequential chromatography on the columns of SP cation exchange HPLC and C18 reverse phase HPLC. The purified BLI-K3 and K4 showed high binding affinity to an anti-bombesin serum (LBE 2G-2) with binding potency of 72 and 95%, respectively, relative to that of bombesin. However, they did not possess any distinctive biological activity of bombesin like peptide. On the contrary, the biological activity of BLI-K5 was similar to that of bombesin but its binding affinity to an anti-bombesin serum was low. The results indicate that three heterogeneous forms of BLI were coexpressed with bombesin and BLI-K2 in the skin of B. orientalis. All forms of the purified BLI in the present study were immunologically active but only BLI-K5 possessed the distinctive biological activity of bombesin like peptide.
