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Die Stereospezifität der Alkoholdehydrogenase

✍ Scribed by C. Bally; F. Leuthardt

Book ID
102856350
Publisher
John Wiley and Sons
Year
1970
Tongue
German
Weight
903 KB
Volume
53
Category
Article
ISSN
0018-019X

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✦ Synopsis

The glyceraldehyde formed by oxidation of glycerol through alcohol dehydrogenase (E.C. 1.1.1.1) from horse liver has been condensed with phosphodihydroxyacetone using either rabbit muscle or liver aldolase. The single product was identified after silylation by gas chromatography as L-sorbose-1-phosphate. No D-fructose-1-phosphate was detected. Apparently liver alcohol dehydrogenase oxidizes glycerol stereospecifically to L-( -)-glyceraldehyde. Thus, the earlier conclusions of Hadorn et al. from chromatography of the borate complexes on Dowex 1 have been confirmed. The same stereospecific behavior was found for both isoenzymes I11 and IV.

With Bis-(trimethylsily1)-trifluoroacetamide L-sorbose-1-phosphate and D-fructose-l-phosphate are persilylated. Two trimethylsilyl groups are bound to the phosphate group. These bonds are not cleaved during gas chromatography.

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Die Stereospezifität der Leberalkoholdeh
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✍ B. Hadorn; F. Leuthardt; E. Ménard; D. Vischer 📂 Article 📅 1963 🏛 John Wiley and Sons 🌐 German ⚖ 345 KB

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