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Enzymatic methods for the determination of tritium at C-1 of d-mannose and at C-3 and C-5 of d-fructose, d-glucose, d-mannose, and their 6-phosphate esters

✍ Scribed by Kevin B. Hicks; Milton S. Feather

Publisher: Elsevier Science
Year: 1980
Tongue: English
Weight: 718 KB
Volume: 105
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(80)90426-1

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✦ Synopsis

Methods have been devised for determining the distribution of carbon-bound tritium at C-l of D-mannose and at C-3 and C-5 of D-glucose, D-fructose, o-mannose, and their 6-phosphate esters using enzymes which, in each case, catalyze the release of tritium into the solvent water, which can be isolated by distillation, and the isotopic content accurately determined. Tritium at C-l of D-mannose is determined by reaction with glucose oxidase. The remaining positions are determined via glycolytic enzymes, with triosephosphate isomerase being used for determining the tritium content at both C-3 and C-5 of both aldoses and Dfructose. The methods involve commercially available enzymes which, in solution, are reasonably stable and minimal chromatographic separation of intermediates. When tested using o-[3-3H]glucose and D-[5-3H]glucose, these methods gave near quantitative results.

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