Purification of an 11 S regulator of the multicatalytic protease.
作者： W Dubiel , G Pratt , K Ferrell , M Rechsteiner
DOI: 10.1016/S0021-9258(18)41681-X
关键词: Enzyme 、 Chemistry 、 Bovine serum albumin 、 Regulator 、 Peptide 、 Protease 、 Red blood cell 、 Lysozyme 、 Hydrolysis 、 Biochemistry
摘要: We have identified and purified a protein complex from human red blood cells that activates the multicatalytic protease (MCP). The complex, which we call regulator, sediments at 11 S is composed of 30-kDa subunits. regulator does not hydrolyze fluorogenic peptides, but when are combined, MCP cleaves succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin Leu-Leu-Glu-p-nitroanilide as much 60-fold faster. Hydrolysis several other peptides stimulated to lesser extent, activated degrade ubiquitin-lysozyme conjugates, bovine serum albumin, or lysozyme. Latent forms display similar sensitivity inhibitors, suggesting activation generate new kinds catalytic sites. In addition, ATP suppresses peptide hydrolysis by latent MCPs same extent. Activation involves binding MCP, migrates slower on native acrylamide gels. Dissociation during prolonged sedimentation glycerol gradients releases active molecules capable being reactivated. Moreover, two-dimensional electrophoresis reveal changes in subunits following activation. Thus, appears result reversible association with MCP.
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