Jan 1, 1993

Isolation of two pyruvate kinase activities in the parasitic protozoan Leishmania mexicana amazonensis

Archives of Biochemistry and Biophysics
Alicia Ponte-SucreJ L Ramirez

Abstract

Using phosphocellulose affinity chromatography we were able to separate two pyruvate kinase (EC 2.7.1.40) activities in the parasitic protozoan Leishmania mexicana amazonesis. One activity (PYK1) showed hyperbolic kinetics and was decreased by fructose 2,6-bisphosphate, whereas the second activity (PYK2) showed sigmoidal kinetics for the substrate phosphoenolpyruvate and was activated by fructose 2,6-bisphosphate. Molecular sieve chromatography (Sephacryl S-400) of PYK1 produced a single peak of apparent molecular mass around 200,000, while PYK2 eluted at a position corresponding to M(r) 55,000.

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Mentioned in this Paper

Fructose 2,6-diphosphate
SDS-PAGE
Leishmania mexicana antigen
Pyruvate Kinase
Protozoa
Pyruvate Kinase Measurement
R-Type Pyruvate Kinase
PTK2B gene
Phosphotransferases
Ion-Exchange Chromatography Procedure

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