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GroEL-like protein complex of thermophilic bacterium Thermus aquaticus.

Abstract：

:GroEL-like particles of Thermus aquaticus are homo-oligomeric complexes of two stacked seven member rings, sedimenting in the gradient at 20S. The apparent molecular mass of the native particles is 820,000 (+/- 30,000). The protein complex is composed with one polypeptide of M(r) 59,000. Immunoblotting results and N-terminal amino acid analysis indicate that the complex is significantly related to the chaperonins. No proteolytic activity was identified in the purified GroEL-like particles. In the presence of Mg2+ and K+ the complex exhibits temperature dependent ATPase activity. Under optimum temperature (75 degrees C) GroEL is stable and hydrolyze ATP with a specific activity of 0.47 mumol min-1 mg-1.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mikulík K,Benada O

doi

10.1006/bbrc.1993.2538

subject

Has Abstract

pub_date

1993-12-15 00:00:00

pages

716-21

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72538-6

journal_volume

197

pub_type

杂志文章

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