Human β-glucosidase: inhibition by sulphates and purification by affinity chromatography on dextran-sulphate-sepharose

Bridget Shafit-Zagardo, Bryan M. Turner

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The acid β-glucosidase (d-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) from human placenta is inhibited by sulphated macromolecules such as Dextran sulphate or chondroitin sulphate. This inhibition is alleviated by compounds such as crude traurocholate or phospholipids, which are known activators of acid β-glucosidase. Partially-purified human β-glucosidase will bind to Dextran sulphate linked to Sepharose 4B and can be eluted with low concentrations of crude sodium taurocholate. This procedure gives a 10-15 fold purification with good yield and has been included in a scheme giving an approx. 4000-fold purification of placental β-glucosidase. Evidence is presented which suggests that phospholipids bind to β-glucosidase by both ionic and hydrophobic interactions. The inhibition of enzyme activity caused by sulphated compounds and non-ionic detergents may be attributed to interference with, respectively, the ionic and hydrophobic binding of phospholipid to the enzyme.

Original languageEnglish (US)
Pages (from-to)7-14
Number of pages8
JournalBBA - Enzymology
Volume659
Issue number1
DOIs
StatePublished - May 14 1981
Externally publishedYes

Fingerprint

Glucosidases
Dextran Sulfate
Affinity Chromatography
Sepharose
Sulfates
Phospholipids
Taurocholic Acid
Acids
Chondroitin Sulfates
Enzymes
Hydrophobic and Hydrophilic Interactions
Detergents
Placenta

Keywords

  • (Human)
  • Affinity chromatography
  • Dextran-sulfate-Sepharose
  • Sulfate inhibition
  • β-Glucosidase

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Human β-glucosidase : inhibition by sulphates and purification by affinity chromatography on dextran-sulphate-sepharose. / Shafit-Zagardo, Bridget; Turner, Bryan M.

In: BBA - Enzymology, Vol. 659, No. 1, 14.05.1981, p. 7-14.

Research output: Contribution to journalArticle

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