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A. Malmström coauthored, with L. Åberg, a 1982 assay for the chondroitin-glucuronate 5-epimerase activity involved in dermatan sulfate biosynthesis. The reaction changes the stereochemical configuration of sugar residues already attached to a polysaccharide, rather than synthesizing a free sugar first.^[ref]

The experiment used chondroitin carrying tritium at the reacting carbon. Release of the label during incubation was measured with a scintillation counter, converting a hard-to-see molecular exchange into a countable assay signal.^[ref]

The preparations also distinguished activities associated with dermatan sulfate and heparan sulfate biosynthesis through different requirements for pH and cofactors. Similar overall epimerization chemistry therefore did not establish that the same enzyme performed both biological tasks.^[ref]

Chondroitin-glucuronate 5-epimerase changes D-glucuronate residues in a chondroitin chain into L-iduronate residues in a dermatan chain. Its classification is EC 5.1.3.19. The reaction alters carbon-5 stereochemistry without adding a sugar residue or changing the residue's elemental formula.^[ref]

This connects polymer modification to dermatan sulfate formation. It is a different enzyme assignment from heparosan-N-sulfate-glucuronate 5-epimerase, whose substrate belongs to another polysaccharide pathway. Similar names do not make the polymer substrates interchangeable.^[ref]

In 1982, A. Malmström and L. Åberg reported distinct uronosyl-epimerase activities associated with dermatan- and heparan-sulfate biosynthesis in microsomal preparations from cultured fibroblasts. The comparison made substrate context experimentally relevant rather than treating all carbon-5 epimerization as one nonspecific activity.^[ref]

For a constructed 50-position substrate segment, conversion of ten eligible glucuronate residues yields ten iduronate residues and 40 unchanged positions. The chain still contains 50 positions. A measurement sensitive only to total sugar amount or shared molecular mass cannot establish that this stereochemical conversion occurred.

L. Åberg coauthored a 1982 investigation of an enzyme involved in making dermatan sulfate. With A. Malmström, L. Åberg used an isotope labelling assay to follow hydrogen exchange during epimerization of residues in chondroitin.^[ref]

The label was tritium attached at carbon five. Material released during incubation was distilled and quantified by liquid-scintillation counting. The study also compared conditions supporting the two epimerase activities present in microsome preparations.^[ref]

The assay illustrates a distinction between a chemical event and the signal used to detect it. Radioactive counts report movement of a label under specified conditions; interpreting them as an enzyme activity requires an appropriate labelled substrate and comparisons for background release. Counting the signal alone would not identify which enzyme produced it.