Electrophoretic separation of neutral and acid β-glucosidase isozymes in human tissues

B. Shafit-Zagardo, E. A. Devine, R. J. Desnick

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Abstract

An electrophoretic system using cellulose acetate has been developed for the resolution of β-glucosidase isozymes (β-D-glucoside glucohydrolase, EC 3.2.1.21 and D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) in human tissue homogenates. Electrophoresis of homogenates from normal and Type I Gaucher disease tissues revealed two fluorescent bands of β-glucosidase activity which corresponded to the acid and neutral isozymes separated by concanavalin A-Sepharose chromatography. The acid isozyme had only β-glucosidase activity, whereas the neutral isozyme also exhibited α-L-arabinosidase (α-L-arabino-furanoside arabinofuranohydrolase, EC 3.2.1.55), β-D-galactosidase (β-D galactoside galactohydrolase, , EC 3.2.1.23) and β-D-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) activities, using the appropriate 4-methylumbelliferyl glycoside. In homogenates of cultured skin fibroblasts, only the acid isozyme was observed which co-electrophoresed with the acidic activity in other tissue homogenates. The acidic activity in tissue and fibroblast homogenates from Type I Gaucher disease appeared to co-electrophorese with the acid isozyme in normal tissues, but had markedly reduced activity.

Original languageEnglish (US)
Pages (from-to)459-465
Number of pages7
JournalBiochimica et biophysica acta
Volume614
Issue number2
Publication statusPublished - Dec 1 1980
Externally publishedYes

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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