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KMID : 0545119990090050655
Journal of Microbiology and Biotechnology
1999 Volume.9 No. 5 p.655 ~ p.660
Isolation of Sphinin,an Inhibitor of Sphingomyelinase,from Streptomyces sp.F50970
Lim Si-Kyu

Park Wan
Abstract
Sphingomyelinase (SMase EC:3.1.4.12) has been suggested to play important roles in the cell cycle, differentiation, apoptosis, inflammation, and the regulation of eukaryotic stress responses. SMase inhibitors may be a powerful tool to elucidate and regulate these cellular responses in which SMase involves. We first isolated an SMase inhibitor, named sphinin, from a strain of soil actinomycetes, F50970. Sphinin inhibited Mg^2+-dependent neutral SMase from chicken embryo at 1.2 §¶/§¢ of IC_50 . Sphinin also inhibited acidic SMase, but it had no inhibitory activity on PI-PLC and PC-PLC, suggesting that sphinin is a specific inhibitor of SMase. The strain F50970 was identified as a Streptomyces sp. by its spiral spore chain, LL-diaminopimelic acid, menaquinone patterns of MK-9 (H`6) and MK-9 (H¢¥8), FA-2c type of fatty acid pattern, and other morphological, physiological, and cultural characteristics.
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