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Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing.

Schurig, H. ; Rutkat, K. ; Rachel, Reinhard ; Jaenicke, R.



Abstract

Enolase (2-phospho-D-glycerate hydrolase; EC 4.2.1.11) from the hyperthermophilic bacterium Thermotoga maritima was purified to homogeneity. The N-terminal 25 amino acids of the enzyme reveal a high degree of similarity to enolases from other sources. As shown by sedimentation analysis and gel-permeation chromatography, the enzyme is a 345-kDa homoctamer with a subunit molecular mass of 48 +/- 5 ...

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