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- W2003823726 abstract "Leukocytes isolated from human blood contain strong α-mannosidase activity. This enzyme has a pH optimum of 4.3 and is unstable by preincubation in citrate buffers at pH's close to the optimum pH of incubation. The Km and Vmax values have been determined with p-nitrophenyl-α-mannopyranoside as substrate. They were higher in acetate buffers than in citrate buffers. The enzyme is highly inhibited by d-mannono-(1→5)lactone (Ki= 90 μM), and shows a subcellular distribution and a structure linked latency compatible with its main localization in primary granules or lysosomes. Reversible inactivation of α-mannosidase is accelerated by EDTA and reversed or prevented by Zn2+. Other cations such as Ag+, Hg2+, Co2+, Fe2+, Fe3+, Cu2+ and Mn2+ accelerate inactivation. Moreover, in an EDTA-treated preparation Zn2+ reactivates the enzyme during assay. It is postulated that human polymorpho-nuclear leukocyte α-mannosidase is a dissociable Zn2+-protein complex in which Zn2+ is essential for enzyme activity." @default.
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- W2003823726 date "1973-09-01" @default.
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- W2003823726 title "Characterization and properties of α-d-mannosidase of human polymorphonuclear leucocytes" @default.
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- W2003823726 doi "https://doi.org/10.1016/0009-8981(73)90265-9" @default.
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