Morphine glucuronide hydrolysis: Superiority of β-glucuronidase from Patella vulgata

J. Combie, J. W. Blake, T. E. Nugent, T. Tobin

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

β-Glucuronidase from Patella vulgata, Helix aspersa, Helix pomatia, and bovine liver were evaluated for usefulness in routine hydrolysis of drug-glucuronic acid conjugates from equine urine samples. Factors affecting the reaction rate (enzyme concentration, ligand concentration, temperature, and pH) were optimized. A 3-h incubation at 65 ° C with 5000 U of β-glucuronidase from P. vulgata per millimeter of urine resulted in complete hydrolysis of all morphine glucuronide in the urine samples. Not only was the enzyme preparation from P. vulgata the most cost-effective β-glucuronidase source studied, but also its thermal stability is such that it can be used at a temperature high enough to substantially shorten the incubation interval. Preliminary work on other drugs that form glucuronide conjugates indicates that this same procedure is similarly superior for use in their hydrolysis.

Original languageEnglish
Pages (from-to)83-86
Number of pages4
JournalClinical Chemistry
Volume28
Issue number1
DOIs
StatePublished - 1982

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, medical

Fingerprint

Dive into the research topics of 'Morphine glucuronide hydrolysis: Superiority of β-glucuronidase from Patella vulgata'. Together they form a unique fingerprint.

Cite this