Paraxin's Action in Shark
NEW YORK AQUARIUM BROOKLYN OSBORN LABSOF MARINE SCIENCES
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A new column chromatography procedure, based on gel-permeation, ion exchange and chromatofocusing was employed to isolate the two 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 toxic, 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 toxins. We have shown that in fish the gill tissue is the main organ for the action of PX. This action is being correlated with the channel-forming activity of PX. Our findings indicate that PX displays a channel or pore activity, e.g., it produces an increase in conductance in an artificial lipid membrane and in liposomes. The interaction of PX with fish gill tissue is being investigated presently.