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

Schurig, H., Rutkat, K., Rachel, Reinhard and Jaenicke, R. (1995) Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. Protein science: a publication of the Protein Society 4 (2), pp. 228-236.

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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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Item type:Article
Date:1995
Institutions:UNSPECIFIED
Identification Number:
ValueType
744388PubMed ID
10.1002/pro.5560040209DOI
Classification:
NotationType
Amino Acid SequenceMESH
Electrophoresis, Polyacrylamide GelMESH
Enzyme ActivationMESH
Enzyme StabilityMESH
Gram-Negative Anaerobic Bacteria/growth & developmentMESH
Hydrogen-Ion ConcentrationMESH
Microscopy, ElectronMESH
Molecular Sequence DataMESH
Molecular WeightMESH
Phosphopyruvate Hydratase/metabolismMESH
Sequence Homology, Amino AcidMESH
Structure-Activity RelationshipMESH
TemperatureMESH
Dewey Decimal Classification:UNSPECIFIED
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Item ID:13268
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