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Multicatalytic and 26 S ubiquitin/ATP‐stimulated proteases in maturing rabbit red blood cells
Author(s) -
Di Cola Domenico,
Pratt Greg,
Rechsteiner Martin
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80222-o
Subject(s) - proteases , protease , percoll , ubiquitin , biochemistry , red blood cell , cytosol , enzyme , biology , proteolysis , lysozyme , chemistry , microbiology and biotechnology , centrifugation , gene
Rabbit red blood cells of various ages were separated on Percoll gradients and the activities of two large cytosolic proteases were measured. Both the multicatalytic protease (MCP), assayed by hydrolysis of fluorigenic peptides, and the 26 S ubiquitin/ATP‐stimulated protease, assayed by degradation of ubiquitin—lysozyme conjugates, declined 3‐fold or less during maturation of rabbit reticulocytes to erythrocytes. The ability of MCP to hydrolyze three classes of peptides decreased in parallel indicating that the 20 S protease is not significantly remodeled during red blood cell maturation.