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A Deficient Pyruvate Kinase with an Electrophoretically Slow‐Moving Component
Author(s) -
Boivin Pierre,
Galand Colette,
Lausecker Charles
Publication year - 1977
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1977.tb02718.x
Subject(s) - pyruvate kinase , denaturation (fissile materials) , chemistry , biochemistry , polyacrylamide gel electrophoresis , urea , enzyme , kinase , pkm2 , mutant , electrophoresis , microbiology and biotechnology , biology , glycolysis , gene , nuclear chemistry
A deficient erythrocyte pyruvate kinase observed in a patient with congenital non‐spherocytic anaemia was characterized by the following properties: very low activity in haemolysates, decreased thermal stability, slightly increased urea denaturation, high affinity for PEP, poor FDP activation, normal ATP inhibition, decreased affinity for ADP, normal pH of optimal activity, and presence of an abnormal slow‐moving component in this layer polyacrylamide gel electrophoresis. The patient was probably double heterozygous for two different deficient mutants of erythrocyte pyruvate kinase.