Membrane-associated protease activity of human erythrocytes.
Membrane-associated protease activity capable of digesting a number of membrane cytoskeletal proteins including band 3 protein was identified in human erythrocytes, almost totally free from contaminating leucocytes and platelets. This enzyme was inhibited by aprotinin (a specific inhibitor for a class of serine protease) and was distinct from the cytosolic calcium-dependent thiol protease (calpain), which is also known to bind to red cell membrane.
Naik
A A
AA
Department of Biochemistry, Goa Medical College.
Chakrabarti
S
S
D010450:Endopeptidases / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism
D008565:Membrane Proteins; D010450:Endopeptidases; D010447:Peptide Hydrolases