Effect of Neuraminidase on the Chromatographic Behaviour of Eleven Acid Hydrolases from Human Liver and Plasma

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Abstract
The elution profile of 11 acid hydrolases from human liver and plasma were directly compared using a system whereby 1 salt gradient was simultaneously applied to 2 DEAE-cellulose chromatographic columns. Plasma .alpha.-L-fucosidase [EC 3.2.1.51], .alpha.-mannosidase [EC 3.2.1.24], .alpha.-galactosidase and .alpha.-glucosidase [EC 3.2.1.20] isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereas .beta.-N-acetylglucosaminidase [EC 3.2.1.30], .beta.-galactosidase [EC 3.2.1.23], .beta.-glucosidase [EC 3.2.1.21], exo-1,4-.beta.-xylosidase [EC 3.2.1.37] and .alpha.-L-arabinofuranosidase [EC 3.2.1.55] isoenzymes were eluted at lower salt concentrations. The elution profiles of .beta.-glucuronidase [EC 3.2.1.31] and acid phosphatase [EC 3.1.3.2] were more complex. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of .beta.-glucosidase, .beta.-xylosidase and acid phosphatase were not altered. Preincubation with neuraminidase had no effect on the elution profiles of 6 liver hydrolases whereas the major isoenzymes of .alpha.-mannosidase, .beta.-galactosidase and .alpha.-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver .alpha.-fucosidase and .alpha.-galactosidase were eluted at slightly lower salt concentrations after incubation with neuraminidase. The results are discussed in relation to the pathogenesis of mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.