Methylthioadenosine phosphorylase activity in human erythrocytes

Amrik Sahota, Dianne R. Webster, Catherine F. Potter, H. Anne Simmonds, A. Victoria Rodgers, Terence Gibson

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

An enzyme capable of degrading 5'-methylthioadenosine to adenine was found in the human erythrocyte. A rapid assay for this enzyme, 5'-methylthioadenosine phosphorylase, was developed using high pressure liquid chromatography. The specific activity in 24 normal subjects was 8.9 ± 2.0 nmol · mg-1 Hb · h-1. Levels within this range were also found in erythrocyte lysates from gouty subjects and patients with a variety of inborn errors of purine metabolism, including patients with a complete deficiency of the adenine salvage enzyme - adenine phosphoribosyltransferase. Erythrocyte lysates from the latter however, were unable to convert the adenine produced to AMP in a linked assay system, in contrast to controls and other patients. These results support the suggestion that adenine, which is excreted in quantity by patients with adenine phosphoribosyltransferase deficiency is derived endogenously from 5'-methylthioadenosine as a by-product of polyamine biosynthesis.

Original languageEnglish (US)
Pages (from-to)283-290
Number of pages8
JournalClinica Chimica Acta
Volume128
Issue number2-3
DOIs
StatePublished - Mar 14 1983
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Clinical Biochemistry
  • Biochemistry, medical

Fingerprint

Dive into the research topics of 'Methylthioadenosine phosphorylase activity in human erythrocytes'. Together they form a unique fingerprint.

Cite this