Alteration in Reactivity of Sphingomyelinase from Streptomyces sp. Modified with a Polyethylene Glycol Derivative

概要

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Purified sphingomyelinase of Streptomyces A9107 (NRRL 15100) was modified with ss-PEG, methoxypolyethyleneglycol succinimidyl succinate, without loss of activity toward sphingomyelin in the mixed micelles with detergents such as sodium deoxycholate and Triton X-100 or toward a water-soluble, synthetic substrate, HNP, 2-(N-hexadecanoylamino)-4-nitrophenyl phosphocholine. The hemolytic and sphingomyelin-hydrolyzing activities of the enzyme toward intact bovine erythrocyte membrane were completely abolished by modification with ss-PEG, whereas the activity toward membranous sphingomyelin in the erythrocyte ghosts was fully retained. The enzyme activity toward liposomal sphingomyelin (large and small unilamellar vesicles) was significantly decreased by PEG-modification. The thermostability of sphingomyelinase was greatly increased by modification with ss-PEG, whereas the sensitivity of the enzyme to proteolysis was not influenced by that modification.
公益社団法人日本薬学会の論文
1993-02-15