Catabolism of thymidine in human blood platelets: purification and properties of thymidine phosphorylase

Biochim Biophys Acta. 1981 Jul 27;654(2):211-8. doi: 10.1016/0005-2787(81)90174-x.


A pyrimidine nucleoside phosphorylase was partially purified from human blood platelets. The purified enzyme, as well as crude enzyme preparations, catalyses the phosphorolysis of thymidine and deoxyuridine, but not of uridine, and is able to catalyse direct pentosyl transfer from these deoxyribonucleosides to uracil or thymine; this enzyme has the properties of a thymidine phosphorylase. It has a molecular weight of about 110,000 and is composed of two identical subunits; it is phosphate dependent, has a maximal activity at a pH value of 5.7, and an isoelectric point of 4.4. This enzyme was mainly of cytoplasmic origin. Although platelet thymidine phosphorylase could promote the degradation or synthesis of thymidine, intact platelets degraded thymidine but were not able to synthesize thymidine from thymine. Blood platelets may play an important role in the degradation of plasma thymidine.

MeSH terms

  • Blood Platelets / metabolism*
  • Cytoplasm / metabolism
  • Deoxyuridine
  • Humans
  • In Vitro Techniques
  • Molecular Weight
  • Pentosyltransferases / blood*
  • Substrate Specificity
  • Thymidine / blood*
  • Thymidine Phosphorylase / blood*


  • Pentosyltransferases
  • Thymidine Phosphorylase
  • Thymidine
  • Deoxyuridine