Stability of enzymes of lysosomal origin in human cerebrospinal fluid

Giancarlo Goi, Alessandra Fabi, Adriana Lombardo, Alberto B. Burlina, Vito Tiby, Anna Visciani, Livia Malesani, Guido Tettamanti

Research output: Contribution to journalArticlepeer-review


The optimal assay conditions and the stability of the following enzymes of lysosomal origin in human cerebrospinal fluid (CSF) were studied: acid phosphatase, β-d-N-acetylglucosarminidase, α-d-galactosidase, β-d-galactosidase, α-d-glucosidase, β-d-glucosidase, α-l-fucosidase, α-d-mannosidase, β-d-glucuronidase. The microsomal α-d-mannosidase, pH 5.7, was used as a reference non-lysosomal glycohydrolase. All the examined enzymes, with the only exception of β-d-glucuronidase, underwent a more or less rapid loss of activity upon CSF storage in the temperature range from 37°C to - 80°C. Storage in liquid nitrogen (-196°C) was the only condition in which full activity for all tested enzymes was maintained for at least 15 days. Addition of human serum albumin to CSF, immediately after withdrawal, had a double effect in favouring enzyme stabilization and causing enzyme activation in some cases, and enzyme inhibition in others. Using conditions warranting enzyme stability the fluorimetric methods for lysosomal enzymes determination in cerebrospinal fluid appear to be highly reproducible (CV <5%) and simple enough for routine use.

Original languageEnglish
Pages (from-to)215-224
Number of pages10
JournalClinica Chimica Acta
Issue number2
Publication statusPublished - Mar 16 1987


  • Fluorimetric enzyme assays
  • Human cerebrospinal fluid
  • Lysosomal enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry


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