What question did this study set out to answer?

Identify and purify an endogenous regulator of the multicatalytic protease from human red blood cells and characterize its mechanism of activation.

November 1, 1992Journal of Biological ChemistryOpen Access

Purification of an 11 S regulator of the multicatalytic protease.

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Authors

WDWolfgang DubielOtto-von-Guericke University Magdeburg GPG PrattUniversity of Utah KFKatherine FerrellLiberty University

Discussion

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Implication

Biochemical analysis demonstrates reversible activation of multicatalytic protease by an 11 S protein complex in human erythrocytes, indicating a non-covalent regulatory mechanism.

Key Points

Identify and purify an endogenous regulator of the multicatalytic protease from human red blood cells and characterize its mechanism of activation.
Purified the 11 S regulator complex composed of 30-kDa subunits from human red blood cells.
Assayed peptidase and proteolytic activity against various fluorogenic peptide substrates and protein targets in the presence and absence of inhibitors and ATP.
Evaluated complex formation and subunit integrity using native polyacrylamide gel electrophoresis, two-dimensional electrophoresis, and glycerol gradient sedimentation.
Combining the 11 S regulator with multicatalytic protease increased the hydrolysis rate of specific fluorogenic peptides up to 60-fold, without enabling degradation of intact proteins like ubiquitin-lysozyme conjugates or bovine serum albumin.
Both latent and activated protease exhibited similar inhibitor sensitivities and equal suppression by ATP.
Activation resulted from reversible, non-covalent binding between the regulator and the protease, as evidenced by slower native gel migration and the recovery of active components after glycerol gradient dissociation.

Cite This Study

Dubiel et al. (1992) studied this question.

synapsesocial.com/papers/6a73d09a76f4fb0e4269f0d7 https://doi.org/10.1016/s0021-9258(18)41681-x

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November 1, 1992Journal of Biological ChemistryOpen Access

Purification of an 11 S regulator of the multicatalytic protease.

View Full Paper

Ask AI

Bookmark

Authors

WDWolfgang DubielOtto-von-Guericke University Magdeburg GPG PrattUniversity of Utah KFKatherine FerrellLiberty University

Discussion

Member takes

Implication

Biochemical analysis demonstrates reversible activation of multicatalytic protease by an 11 S protein complex in human erythrocytes, indicating a non-covalent regulatory mechanism.

Key Points

Identify and purify an endogenous regulator of the multicatalytic protease from human red blood cells and characterize its mechanism of activation.
Purified the 11 S regulator complex composed of 30-kDa subunits from human red blood cells.
Assayed peptidase and proteolytic activity against various fluorogenic peptide substrates and protein targets in the presence and absence of inhibitors and ATP.
Evaluated complex formation and subunit integrity using native polyacrylamide gel electrophoresis, two-dimensional electrophoresis, and glycerol gradient sedimentation.
Combining the 11 S regulator with multicatalytic protease increased the hydrolysis rate of specific fluorogenic peptides up to 60-fold, without enabling degradation of intact proteins like ubiquitin-lysozyme conjugates or bovine serum albumin.
Both latent and activated protease exhibited similar inhibitor sensitivities and equal suppression by ATP.
Activation resulted from reversible, non-covalent binding between the regulator and the protease, as evidenced by slower native gel migration and the recovery of active components after glycerol gradient dissociation.

Cite This Study

Dubiel et al. (1992) studied this question.

synapsesocial.com/papers/6a73d09a76f4fb0e4269f0d7 https://doi.org/10.1016/s0021-9258(18)41681-x

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