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- W2034196306 abstract "A radioimmunoassay capable of measuring nanogram quantities of Arthrobacter sialophilus neuraminidase was developed. Neuraminidases from several influenza viruses, Clostridium perfringens, Vibrio cholerae, Diplococcus pneumoniae, several group B streptococcal isolates, and human fibroblasts each failed to react with antisera raised in guinea pigs against the homogeneous A. sialophilus enzyme. Cross-reactivity was limited to neuraminidases from other Arthrobacter isolates and weakly, also with a Corynebacterium diphtheria enzyme preparation. Among the Arthrobacter-derived enzymes examined, that obtained from A. ureafaciens appeared nearly identical by this immunochemical criterion. Other designated Arthrobacter strains produced isofunctional proteins which exhibited distinct serological differences. The monospecific antibody also inhibited enzymatic activity of Arthrobacter neuraminidases. In the case of enzyme from A. sialophilus, inhibition by homologous antibody ranged from almost complete with Collocalia mucoid (a high-molecular-weight substrate) to none using sialyllactose. This substrate-dependent differential inhibition supports a steric model for inhibition of enzyme catalysis. Each of the cross-reacting Arthrobacter enzymes showed differential inhibition with sialyllactose, indicating variation in the positioning of one or more determinants with respect to their active sites. Further applications for this radioimmunoassay in relation to the use of neuraminidase in cell and molecular biology are discussed." @default.
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- W2034196306 date "1980-07-01" @default.
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- W2034196306 title "Radioimmunoassay of Arthrobacter neuraminidase: Applications to catalytic and taxonomic studies" @default.
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- W2034196306 doi "https://doi.org/10.1016/0003-2697(80)90566-7" @default.
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