Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.

摘要: The glycolytic enzyme enolase (EC 4.2.1.11) is active as dimers formed from three subunits encoded by different genes. embryonic alphaalpha isoform remains distributed in many adult cell types, whereas a transition towards betabeta and gammagamma isoforms occurs striated muscle cells neurons respectively. It not understood why exhibits tissue-specific with very close functional properties. We approached this problem the purification of native betabeta-enolase mouse hindlimb muscles raising specific antibodies high titre against protein. These reagents have been useful revealing heterogeneity beta-enolase subunit that changes vivo vitro maturation. A basic carboxypeptidase appears to be involved generating an acidic variant, may regulate plasminogen binding subunit. show for first time pure binds affinity adjacent enzymes pathway (pyruvate kinase phosphoglycerate mutase), favouring hypothesis these form segment. betabeta-Enolase sarcomeric troponin but actin tropomyosin. Some properties are shared alphaalpha-isoenolase, which also expressed muscle, neuron-specific gammagamma-enolase. results support idea interactions macromolecules will address at subcellular site where ATP, produced through glycolysis, most needed contraction. Such targeting could modulated post-translational modifications.