Korean J Physiol Pharmacol.  1998 Oct;2(5):637-644.

Further characterization of bombesin like immunoreactivities from the skin of Korean fire-bellied toad, Bombina orientalis

Affiliations
  • 1Department of Physiology College of Medicine, Hallym University, Chunchon, Kangwon-Do 200-702, Korea.
  • 2Department of Anatomy, College of Medicine, Hallym University, Chunchon, Kangwon-Do 200-702, Korea.

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.

Keyword

Bombesin; Bombesin like immunoreactivity; Frog skin peptide; Molecular; heterogeneity; Gastric release; Pancreatic exocrine secretion obligation
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