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Clinical Chemistry 43: 45-51, 1997;
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(Clinical Chemistry. 1997;43:45-51.)
© 1997 American Association for Clinical Chemistry, Inc.

Articles

Determination of xylosyltransferase activity in serum with recombinant human bikunin as acceptor

Christian Weilke, Thomas Brinkmann and Knut Kleesieka

Institut für Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein-Westfalen, Universitätsklinik der Ruhr-Universität Bochum, Georgstr. 11, 32545 Bad Oeynhausen, Germany.
a Author for correspondence. Fax +49 5731 972307; e-mail HDZ.ILTM{at}post.uni-bielefeld.de

Xylosyltransferase (XT) is the chain-initiating enzyme of the biosynthesis of chondroitin sulfate. So far, XT activity has been detected by incorporation of [14C]xylose in chemically deglycosylated cartilage proteoglycan or silk fibroin. However, these acceptors allow no reliable determination in blood. We found that recombinant bikunin is an excellent acceptor for XT. The Michaelis–Menten constants for the xylosylation of silk, deglycosylated cartilage proteoglycans, and bikunin were 545, 155, and 0.9 µmol/L, respectively. With recombinant bikunin as acceptor, we developed a sensitive assay that allows a precise determination of XT activity in serum. We measured the serum XT activities of 500 blood donors and observed a considerable sex and age dependence. XT activities in men (0.77–1.50 mU/L) were ~30% higher than in women (0.58–1.20 mU/L) and reached a maximum in donors of ~40 years of age. During the menstrual cycle, serum XT activity showed a significant coincidence with the ß-estradiol concentration, and in the first trimester of pregnancy we observed a strong increase in serum XT activity.


Key Words: indexing terms: glycosyltransferases • proteochondroitin sulfates • glycoproteins • xylose • estradiol




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