A. J. Padgett-McCue coauthored a 2000 study identifying a chondroitin synthase and establishing what polysaccharide it made. The work connected an enzyme with the alternating glucuronic acid and N-acetylgalactosamine units of chondroitin. The characterized protein carried both sugar-transfer activities required to extend this repeating chain.[ref]
Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F by P. L. DeAngelis and A. J. Padgett-McCue. Abstract, Journal of Biological Chemistry 275 (2000), pp. 24124–24129; DOI 10.1074/jbc.M003385200.
The experimental reasoning combined nucleotide sugar specificity, size-exclusion chromatography and selective enzymatic digestion of the product. This gives a useful example of complementary measurements: a large molecular size establishes that a polymer was made, but does not identify its repeating chemical structure. Agreement between the sugar composition and the response to a chondroitin-cleaving enzyme supplied more specific evidence. The contribution is therefore a chemically tested biosynthetic assignment, rather than a prediction based only on similarity between protein sequences.[ref]
Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F by P. L. DeAngelis and A. J. Padgett-McCue. Abstract: donor specificity, gel filtration and contrasting lyase susceptibility.
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