Purification and characterisation of chicken brain hypoxanthine-guaninephosphoribosyltransferase

Gabor Veres, E. Monostori, I. Raskó

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Hypoxanthine-guanine phosphoribosyltransferase enzyme (EC 2.4.2.8) from chicken brain has been purified 10000-fold to homogeneity. The molecular mass of the native enzyme is 85 kDa, with four subunits, each of 26 kDa, and exerts its maximum activity at pH 10.0. The Km values for hypoxanthine and guanine are 5.2 and 1.8 μM, respectively. The half-life of the enzyme is 30 min at 85°C. Monoclonal antibodies were raised against the native purified enzyme and were used for purification of enzyme to homogeneity. The monoclonal antibody did not bind to the active centre of the enzyme.

Original languageEnglish
Pages (from-to)299-303
Number of pages5
JournalFEBS Letters
Volume184
Issue number2
DOIs
Publication statusPublished - May 20 1985

Fingerprint

Hypoxanthine
Purification
Chickens
Brain
Enzymes
Monoclonal Antibodies
Hypoxanthine Phosphoribosyltransferase
Guanine
Molecular mass
Half-Life

Keywords

  • Enzymology HGPRT Chicken Monoclonal antibody

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification and characterisation of chicken brain hypoxanthine-guaninephosphoribosyltransferase. / Veres, Gabor; Monostori, E.; Raskó, I.

In: FEBS Letters, Vol. 184, No. 2, 20.05.1985, p. 299-303.

Research output: Contribution to journalArticle

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