| pubmed-article:7151276 | pubmed:abstractText | Pyruvate kinase (PK) has been purified from the red blood cells of two sisters who had suffered severe chronic non-spherocytic haemolytic anaemia since infancy, and of one patient who had haemolytic anaemia during pregnancy. The two sisters showed remarkable clinical improvement following splenectomy. The enzyme from their red cells was found to exhibit low activity (about 25% of normal) in crude haemolysates, low affinity for the substrate, phosphoenol pyruvate (PEP), and high sensitivity to fructose-1,6-diphosphate (FDP) activation. This PK differs from previously reported variants and it is provisionally designated PK 'Torre Annunziata'. The enzyme from the other patient had near-normal activity in crude haemolysates, slight changes in kinetics with respect to the substrate, PEP, and with respect to the effects of FDP, ATP and pH, and a markedly reduced thermostability. This PK also differs from previously reported variants and it is provisionally designated PK 'Torre del Greco'. During the course of this study an improved method for purification of PK using Cibacron blue sepharose has been developed. | lld:pubmed |
