졸복 (Takifugu pardalis)과 가무락조개 (Cyclina sinensis)로부터 항균성 펩타이드 정제 및 특성

Abstract

Purification and characterization of antimicrobial peptides from the hemolymph of the venus clam (Cyclina sinensis)

Tae Young Kim

Department of Biotechnology, Graduate School, Pukyong National University

Abstract Two antimicrobial peptides were purified from the hemolymph of the venus clam (Cyclina sinensis). To purify the antimicrobial peptide, the acidic extract was partially purified with Sep-Pak C18 solid phase extraction cartridges using stepwise gradient while increasing the percent of methanol (60%) containing 0.1% TFA. Antimicrobial activity was recovered in the 60% methanol fraction and this fraction was further purified by cation-exchange and C18 reversed-phase high performance liquid chromatography. The two purified peptides were exhibited potent antimicrobial activity against gram-positive bacteria, B.subtilis. To investigate the primary structure of two purified peptides, the molecular weight and amino acid sequence analysis were performed by MALDI-TOF MS and Edman degradation. The molecular weight and primary sequence of VP1 was 3838.296 Da and 25 amino acids. The molecular weight and primary sequence of VP2 was 3852.243 Da and 15 amino acids.