Abstract
A naturally occurring hemolysin (HL) was detected in the serum of the hermit crab Clibanarius longitarsus using mammalian RBC as indicator cells. The serum gave the highest HL titer with rabbit RBC. Cross adsorption of C. longitarsus serum with fixed rabbit RBC resulted in the complete removal of the lytic activity from the serum. The hemolytic activity in the serum of C. longitarsus was independent of divalent cations, reversibly sensitive to EDTA, thermolabile, stable between the pH 6-8. Further studies demonstrated that the HL activity is proteinaceous as it was precipitable by conventional deproteinizing agents and susceptible to the action of proteases and 2-mercapthoethanol. The HL-inhibition assay performed with several carbohydrates (mono, di, oligo, polysaccharides and Lipo polysaccharides) revealed that the serum HL was capable of specifically recognizing laminarin (a homopolymer of β 1, 3-glucan). Thus this hemolysin appears to be unique among all the known crustacean hemolysins.
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