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

Abstract

The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE‐cellulose chromatographic columns. Plasma α‐L‐fucosidase, α‐mannosidase, α‐galactosidase and α‐glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereas β‐N‐acetyl‐glucosaminidase, β‐galactosidase, β‐glucosidase, exo‐1,4‐β‐xylosidase and α‐L‐arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of β‐glucuronidase and acid phosphatase were more complex. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of β‐glucosidase, β‐xylosidase and acid phosphatase were not altered. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of α‐mannosidase, β‐galactosidase and α‐L‐arabinofuranosidase were eluted at markedly lower salt concentrations. Liver α‐fucosidase and α‐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. Copyright © 1977, Wiley Blackwell. All rights reserved