Assay of fumarylacetoacetate fumarylhydrolase in human liver-deficient activity in a case of hereditary tyrosinemia.

Abstract

The activity of human liver fumarylacetoacetate fumarylhydrolase (EC 3.7.1.2) has been determined with fumarylacetoacetate as substrate. The Km was found to be 1.3 mu mol/l. Subcellular fractionation showed localization of the enzyme in the particle-free supernatant (cytosol). ZnCl2, CuCl2 and p-chloromercuribenzoic acid had a marked inhibitory effect on the enzyme activity, but no inhibition was observed with a number of anions and substrate analogs. Fumarylacetoacetate fumarylhydorlase activity in liver tissue from a patient with hereditary tyrosinemia was found to be less 2% of the controls. The assay is applicable to 3 mg of liver tissue which may be obtained by needle biopsy.

• Authors: E A Kvittingen, E Jellum, O Stokke
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 115 Issue 3 Pg. 311-9 (Sep 1981) ISSN: 0009-8981 [Print] Netherlands
• PMID: 7296877 (Publication Type: Journal Article)

Chemical References

• Acetoacetates
• Fumarates
• Tyrosine
• Hydrolases
• fumarylacetoacetase

Topics

• Acetoacetates (analysis, deficiency)
• Adult
• Aged
• Amino Acid Metabolism, Inborn Errors (enzymology)
• Cell Fractionation
• Cytosol (enzymology)
• Drug Stability
• Fumarates (analysis, deficiency)
• Humans
• Hydrolases (analysis, deficiency)
• Infant
• Kinetics
• Liver (enzymology)
• Middle Aged
• Tyrosine (blood)