Purification and partial characterization of neuraminidase from type III group B streptococci.
Extracellular neuraminidase from a type III fresh clinical isolate of a group B streptococcus was purified by a combination of salt fractionation, affinity chromatography of Affi-Gel blue, ion-exchange chromatography on diethylaminoethylcellulose, and gel filtration on Sephacryl S-200. These procedures yielded enzyme which was purified approximately 1,000-fold compared with the enzyme found in the original supernatant fluid. This type III streptococcal neuraminidase had a molecular weight of approximately 125,000 as estimated by filtration on Sephacryl S-200 and approximately 106,000 when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In contrast to the majority of other bacterial neuraminidases, the type III group B streptococcal enzyme had no effect on colominic acid or N-acetylneuramin-lactose; however, it was quite active on bovine submaxillary mucin.
D002845:Chromatography; D002850:Chromatography, Gel; D007785:Lactose / Q000031:analogs & derivatives / Q000378:metabolism; D008970:Molecular Weight; D009439:Neuraminidase / Q000302:isolation & purification* / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D012794:Sialic Acids / Q000378:metabolism; D013292:Streptococcus agalactiae / Q000201:enzymology*; D013379:Substrate Specificity
D011134:Polysaccharides; D012794:Sialic Acids; C000020:N-acetylneuraminoyllactose; C014420:colominic acid; D009439:Neuraminidase; D007785:Lactose