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- W2011799455 abstract "Streptomyces mannosidase, like the enzyme from other sources, is shown to require a divalent cation for enzyme activity. N-Ethylmaleimide pretreatment of enzyme-containing cells eliminated the requirement of aeration for enzyme activity. Methyl-α-D-mannoside was found to be a strong inhibitor of the hydrolysis of both p-nitrophenyl-α-D-mannoside and mannosidost reptomycin. The enzyme is bound at or near the surface of the cell and is inactivated by sonic oscillation. Small participate matter containing most of the activity can be released from the cells into water, such release being inhibited by phosphate, Tris, or sodium chloride." @default.
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- W2011799455 date "1970-03-01" @default.
- W2011799455 modified "2023-09-23" @default.
- W2011799455 title "Location and action ofStreptomyces griseus ?-D-mannosidase, an antibiotic-transforming enzyme" @default.
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- W2011799455 doi "https://doi.org/10.1002/bit.260120203" @default.
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