Oct 1, 1975

D-glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure

Hoppe-Seyler's Zeitschrift für physiologische Chemie
H E Pauly, G Pfleiderer


1) Glucose dehydrogenase from Bacillus megaterium has been purified to a specific activity of 550 U per mg protein. The homogeneity of the purified enzyme was demonstrated by gel electrophoresis and isoelectric focusing. 2) The amino acid composition has been determined. 3) The molecular weight of the native enzyme was found to be 116000 by gel permeation chromatography, in good agreement with the values of 120000 and 118000, which were ascertained electrophoretically according to the method of Hedrick and Smith and by density gradient centrifugation, respectively. 4) In the presence of 0.1% sodium dodecylsulfate and 8M urea, the enzyme dissociates into subunits with a molecular weight of 30000 as determined by dodecylsulfate gel electrophoresis. These values indicate that the native enzyme is composed of four polypeptide chains, each probably possessing one coenzyme binding site, which can be concluded from fluorescent titration of the NADH binding sites. 5) In polyacrylamide disc electrophoresis, samples of the purified enzyme exhibit three bands of activity, which present the native (tetrameric) form of glucose dehydrogenase and two monomeric forms (molecular weight 30000), arising under the conditions of pH and ionic streng...Continue Reading

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Mentioned in this Paper

Alcohol Oxidoreductases
Structure-Activity Relationship
Glucose, (beta-D)-Isomer
Sulfhydryl Reagents
Bacillus megaterium
Hydrogen-Ion Concentration

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