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Cytosolic calcium dependent neutral proteinase of human erythrocytes: The role of calcium ions on the molecular and catalytic properties of the enzyme

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
107
Issue
3
Identifiers
DOI: 10.1016/0006-291x(82)90628-3
Disciplines
  • Biology

Abstract

Abstract The soluble neutral proteinase of human erythrocytes dissociates into constituent subunits of 80k and 30k in the presence of mM concentrations of Ca 2+. Similarly the soluble natural inhibitor of this proteinase, of approximate molecular weight 240k, is dissociated into 60k subunits by mM concentrations of Ca 2+. Removal of Ca 2+ restores the native oligomeric structure of the proteinase and of the natural inhibitor. The formation of the native active enzyme or of the inactive enzyme-inhibitor complex depends on reversible association-dissociation processes mediated by Ca 2+ concentration.

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