Xylosyltransferase II is the predominant isoenzyme which is responsible for the steady-state level of xylosyltransferase activity in human serum

Biochemical and Biophysical Research Communications

Volumn 459, Issue 3, 2015, Pages 469-474

  Kuhn, Joachim ^a   Götting, Christian ^b   Beahm, Brendan J ^c   Bertozzi, Carolyn R ^c   Faust, Isabel ^a   Kuzaj, Patricia ^a   Knabbe, Cornelius ^a   Hendig, Doris ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b MVZ Labor Limbach Nürnberg ^*  (Germany)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

Glycosaminoglycan; Human serum; Mass spectrometry; Proteoglycan; Xylosyltransferase

Indexed keywords

GLYCOSYLTRANSFERASE; ISOENZYME; PROTEOGLYCAN; RECOMBINANT PROTEIN; SERINE; UDP XYLOSE-PROTEIN XYLOSYLTRANSFERASE; URIDINE DIPHOSPHATE XYLOSE; XYLOSE;

ANALOGS AND DERIVATIVES; BIOSYNTHESIS; BLOOD; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; METABOLISM; TANDEM MASS SPECTROMETRY;

CATALYTIC DOMAIN; CELL LINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMANS; ISOENZYMES; MODELS, MOLECULAR; PENTOSYLTRANSFERASES; PROTEOGLYCANS; RECOMBINANT PROTEINS; SERINE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUBSTRATE SPECIFICITY; TANDEM MASS SPECTROMETRY; URIDINE DIPHOSPHATE XYLOSE; XYLOSE;

EID: 84931400118     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.02.129     Document Type: Article

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