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Accessible Unlicensed Requires Authentication Published by De Gruyter June 1, 2005

Purification and Characterization of the 20S Proteasome from Ostrich Skeletal Muscle

A. R. Thomas, V. Oosthuizen, R. J. Naudé and K. Muramoto
From the journal


The proteasome is a high molecular weight, multisubunit and multicatalytic enzyme. Here we report the purification and characterization of ostrich skeletal muscle 20S proteasome. It was purified to homogeneity with Mr 700 000, pI 6.67 and a ladder of 22.2 33.5 kDa bands on SDSPAGE. The amino acid composition and aminoterminal sequences showed large identities to those of other species. For the three major activities, pH and temperature optima ranged between 8.0 11.0 and 40 70C, and stabilities between 5 12 and up to 40 60C. Substrate specificity and inhibitory effects were also studied. Many similarities to other sources were shown, with a few significant differences.

Published Online: 2005-06-01
Published in Print: 2002-08-27

Copyright © 2002 by Walter de Gruyter GmbH & Co. KG