Isolation of a human thiopurine S-methyltransferase (TPMT) complementary DNA with a single nucleotide transition A719G (TPMT*3C) and its association with loss of TPMT protein and catalytic activity in humans.

doi:10.1016/S0009-9236(98)90021-2

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Article

Isolation of a human thiopurine S-methyltransferase (TPMT) complementary DNA with a single nucleotide transition A719G (TPMT*3C) and its association with loss of TPMT protein and catalytic activity in humans.

Clinical pharmacology and therapeutics - 1 Jul 1998

Loennechen T, Yates C R, Fessing M Y, Relling M V, Krynetski E Y, Evans W E

Abstract excerpt

OBJECTIVE: Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes the S-methylation of mercaptopurine, azathioprine, thioguanine and most of their nucleotide metabolites. TPMT exhibits genetic polymorphism, with about 10% of individuals having intermediate TPMT activity becaus...

Topics

Adult
Blotting, Western
Child
Child, Preschool
DNA, Complementary
Genotype
Humans
Introns
Male
Methyltransferases
Point Mutation
Polymerase Chain Reaction

Source

Open in PubMed

Identifiers

PMID: 9695718
DOI: 10.1016/S0009-9236(98)90021-2

Genes

TPMT

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9695718-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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