Multicatalytic and 26 S ubiquitin/ATP-stimulated proteases in maturing rabbit red blood cells.
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.
Di Cola
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D
Institute of Biochemical Science, Faculty of Medicine, University of Chieti, Italy.
Pratt
G
G
Rechsteiner
M
M
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D002499:Centrifugation, Density Gradient; D003546:Cysteine Endopeptidases / Q000097:blood*; D003600:Cytosol / Q000201:enzymology; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000097:blood*; D011205:Povidone; D046988:Proteasome Endopeptidase Complex; D011817:Rabbits; D012822:Silicon Dioxide; D014452:Ubiquitins / Q000097:blood*
D009097:Multienzyme Complexes; D014452:Ubiquitins; C016039:Percoll; D012822:Silicon Dioxide; D000255:Adenosine Triphosphate; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D011205:Povidone