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Partial HGPRT‐deficiency in a patient with the Lesch‐Nyhan syndrome: Evidence for a structural mutation affecting the PRPP binding site
Author(s) -
Rijksen G.,
Staal G. E. J.,
der Vlist M. J. M.,
Beemer F. A.,
Troost J.,
Laarhoven J. P. R. M.,
Bruyn C. H. M. M.
Publication year - 1981
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf02263643
Subject(s) - lesch–nyhan syndrome , hypoxanthine guanine phosphoribosyltransferase , mutation , chemistry , microbiology and biotechnology , biology , biochemistry , mutant , gene
The residual HGPRT activity in a patient with the Lesch‐Nyhan syndrome was 10–15% in haemolysate and about 30% in fibroblast lysate. Due to a structural mutation affecting the PRPP site of the enzyme (increased K m PRPP, absence of product inhibition, absence of stabilization by PRPP) the in vivo activity in intact erythrocytes was negligible.