Unit

UNIT 21.6 Purification of the Eukaryotic 20S Proteasome

  1. Sherwin Wilk,
  2. Wei-Er Chen

Published Online: 1 NOV 2001

DOI: 10.1002/0471140864.ps2106s25

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Wilk, S. and Chen, W.-E. 2001. Purification of the Eukaryotic 20S Proteasome. Current Protocols in Protein Science. 25:21.6:21.6.1–21.6.9.

Author Information

  1. Mount Sinai School of Medicine, New York, New York

Publication History

  1. Published Online: 1 NOV 2001
  2. Published Print: SEP 2001

Abstract

The 20S proteasome is the catalytic core of the major extralysosomal proteolytic system of the cell. Combination of the 20S proteasome with a complex of regulatory proteins forms the 26S proteasome, which in turn is responsible for the recognition and degradation of ubiquitin-protein conjugates. As described in this unit, the constitutive form of the 20S proteasome can be conveniently purified as a stable and homogeneous preparation from bovine pituitaries. A support protocol details an enzyme assay used in evaluating proteasomal activity. The 20S proteasome is the catalytic core of the major extralysosomal proteolytic system of the cell.