Pardaxin's Action in Shark
NEW YORK AQUARIUM BROOKLYN OSBORN LABSOF MARINE SCIENCES
Pagination or Media Count:
A new column chromatograph procedure, based on gel-permeation, ion exchange and chromatofocusing was employed to isolate the tow main proteaceous, toxic, cytolytic and pore forming factors from the gland secretion of the Red Sea flatfish Pardachirus marmoratus. Pardaxin IPXI consisting 10 of the gland protein secretion, was shown to be 5-10 times more oxic, cytolytic and active on pore formation than pardaxin II PXII 8 of gland protein secretion. Gel- electrophoresis, amino acid analysis and N-terminal amino acid sequencing reveals a high degree of homogeneity and resemblance between the two toxions. They are rich in serine, glycine, alanine, leucine, and phyenylalanine and devoid of arginine and tryptophan. Their N-terminal was found to be NH2-Gly-Phe- Phe. Their hydrophobicity if evident from the chromatographic behavior on a hydrophobic resin, presence of nine successive hydrophobic residues on the NH2- terminal, overall percentage of toxins hydrophobicity and decreament of aqueous drops volume. Pardaxin I was iodinated without affecting its chemical and pore forming properties. It binds to liposomes, of different phospholipid compositions. We have shown that in fish the gill tissue is the main organ for the action of PX.