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Purification and characterisation of chicken brain hypoxanthine‐guaninephosphoribosyltransferase
Author(s) -
Veres Gabor,
Monostori Eva,
Rasko Istvan
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80626-8
Subject(s) - hypoxanthine , chemistry , chromatography , biochemistry , enzyme
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 K m 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.