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Pyruvate kinase activity and response to allosteric effectors in rat erythrocytes and reticulocytes fractionated by multiple partitioning in aqueous two‐phase systems
Author(s) -
Pinilla Montserrat,
RodriguezHorche Paz,
Luque Jose
Publication year - 1987
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290050409
Subject(s) - pyruvate kinase , allosteric regulation , effector , chemistry , aqueous solution , pkm2 , biochemistry , phase (matter) , kinase , microbiology and biotechnology , biology , enzyme , glycolysis , organic chemistry
Specific activity of pyruvate kinase decreases as the age of rat erythrocytes increases in fractions obtained by counter‐current distribution in dextran‐polyethylene glycol biphasic systems; the enzyme is inhibited by ATP and activated by fructose‐1,6‐bisphosphate at low phosphoenol pyruvate concentrations. Specific activity does not change in fractions from > 95 per cent‐rich reticulocytes (anaemic rats); the enzyme is inhibited by ATP but not activated by fructose‐1,6‐bisphosphate. These results can be explained on the basis of different pyruvate kinase isozymes and suggest that decrease in activity is not affecting regulatory properties during erythrocytes aging.