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. 1969 Jun;98(3):924–929. doi: 10.1128/jb.98.3.924-929.1969

α-l-Fucosidase from a Soil Bacterium

K Mortensson-Egnund 1,2, R Schöyen 1,2, C Howe 1,2, L T Lee 1,2, A Harboe 1,2
PMCID: PMC315275  PMID: 4239704

Abstract

Intracellular glycosidases were measured in cell-free extracts obtained by ultrasonic disruption of a gram-negative soil coccobacillus (Chase, 1938). From these extracts, α-l-fucosidase was purified about 120-fold by salting out with (NH4)2SO4, ion exchange chromatography, and gel filtration. The approximate molecular weight of the enzyme was 50,000; its pH optimum was 5. The enzyme was inhibited by l-fucose and split this sugar from a purified acid mucopolysaccharide from chicken chorioallantoic fluid. The acid mucopolysaccharide is identical with a component (host antigen) of the hemagglutinin of influenza virus. Its antigenic reactivity is altered by cell-free extracts of the bacterium, in which the responsible enzyme is thought to be an α-l-fucosidase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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