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G6PD Hillbrow: A New Variant of Glucose‐6‐Phosphate Dehydrogenase Associated with Drug‐induced Haemolytic Anaemia
Author(s) -
Cayanis Eftihia,
Gomperts E. D.,
Balinsky Doris,
Disler P.,
Myers A.
Publication year - 1975
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1975.tb00550.x
Subject(s) - enzyme , glucose 6 phosphate dehydrogenase , thermostability , chemistry , dehydrogenase , red cell , glucose 6 phosphate dehydrogenase deficiency , biochemistry , enzyme assay , michaelis–menten kinetics , red blood cell , phosphate , medicine
S ummary . A new genetic variant of the red cell enzyme glucose‐6‐phosphate dehydrogenase is described. It was observed in a patient presenting with severe haemolytic anaemia and renal failure following ingestion of an overdose of Beserol (paracetamol and chlormezanone). The enzyme in the red cell had 12% of the activity of a normal B + control, but only slightly lower activity in the kidney compared with a normal control. The red cell enzyme showed normal electrophoretic mobility and thermostability, a biphasic pH optimum curve, higher than normal utilization of the substrate analogues 2‐deoxyglucose‐6‐phosphate and deamino‐NADP, and lower than normal Michaelis constants for both substrates, glucose‐6‐phosphate and NADP. The enzyme was strongly inhibited in vitro by high concentrations of paracetamol and chlormezanone. The extent of inhibition was similar to that for the enzyme from a normal B + individual.