Alpha-L-fucosidase from a soil bacterium.
Intracellular glycosidases were measured in cell-free extracts obtained by ultrasonic disruption of a gram-negative soil coccobacillus (Chase, 1938). From these extracts, alpha-l-fucosidase was purified about 120-fold by salting out with (NH(4))(2)SO(4), 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 alpha-l-fucosidase.
D001419:Bacteria / Q000201:enzymology*; D002474:Cell-Free System; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005643:Fucose / Q000378:metabolism / Q000494:pharmacology; D006025:Glycosaminoglycans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012988:Soil Microbiology
D006025:Glycosaminoglycans; D005643:Fucose; D006026:Glycoside Hydrolases