Cytosolic calcium dependent neutral proteinase of human erythrocytes: the role of calcium ions on the molecular and catalytic properties of the enzyme |
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Authors: | E Melloni B Sparatore F Salamino M Michetti S Pontremoli |
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Affiliation: | Institute of Biological Chemistry, University of Genoa, Genoa, Italy. |
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Abstract: | The soluble neutral proteinase of human erythrocytes dissociates into constituent subunits of 80k and 30k in the presence of mM concentrations of Ca2+. Similarly the soluble natural inhibitor of this proteinase, of approximate molecular weight 240k, is dissociated into 60k subunits by mM concentrations of Ca2+. Removal of Ca2+ 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 Ca2+ concentration. |
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Keywords: | CDSNP calcium-dependent soluble neutral proteinase EGTA ethylene glycol bis (β-amino-ethyl ether) N, N′-tetra acetic acid IAA iodoacetic acid Cm car?ymethyl |
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