Purification and characterization of the 20S proteasome from ostrich skeletal muscle

Adele R. Thomas; Vaughan Oosthuizen; Ryno J. Naudé; Koji Muramoto

doi:10.1515/BC.2002.141

Purification and characterization of the 20S proteasome from ostrich skeletal muscle

Adele R. Thomas, Vaughan Oosthuizen, Ryno J. Naudé, Koji Muramoto

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

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 M_r 700 000, pl 6.67 and a 'ladder' of 22.2-33.5 kDa bands on SDS-PAGE. The amino acid composition and amino-terminal 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 40-70°C, and stabilities between 5-12 and up to 40-60°C. Substrate specificity and inhibitory effects were also studied. Many similarities to other sources were shown, with a few significant differences.

Original language	English
Pages (from-to)	1267-1270
Number of pages	4
Journal	Biological Chemistry
Volume	383
Issue number	7-8
DOIs	https://doi.org/10.1515/BC.2002.141
Publication status	Published - 2002 Jul 1

Keywords

Inhibitory
Kinetic
Multicatalytic
Subunits

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Clinical Biochemistry

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10.1515/BC.2002.141

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abstract = "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, pl 6.67 and a 'ladder' of 22.2-33.5 kDa bands on SDS-PAGE. The amino acid composition and amino-terminal 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 40-70°C, and stabilities between 5-12 and up to 40-60°C. Substrate specificity and inhibitory effects were also studied. Many similarities to other sources were shown, with a few significant differences.",

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AU - Thomas, Adele R.

AU - Oosthuizen, Vaughan

AU - Naudé, Ryno J.

AU - Muramoto, Koji

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AB - 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, pl 6.67 and a 'ladder' of 22.2-33.5 kDa bands on SDS-PAGE. The amino acid composition and amino-terminal 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 40-70°C, and stabilities between 5-12 and up to 40-60°C. Substrate specificity and inhibitory effects were also studied. Many similarities to other sources were shown, with a few significant differences.

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Purification and characterization of the 20S proteasome from ostrich skeletal muscle

Abstract

Keywords

ASJC Scopus subject areas

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