Journal article
Comparison of N-glycosides of fetuins from different species and human alpha 2-HS-glycoprotein
Biochemistry (Easton), Vol.31(20), pp.4915-4921
05/26/1992
DOI: 10.1021/bi00135a024
PMID: 1375510
Abstract
Complex type N-glycosides of commercial bovine fetuin preparations from pooled fetal calf serum have been shown to contain comparable amounts of Gal4,4,4TRI (see structure A below) and Gal4,4,3TRI (structure B) as major asialo-structures. To investigate whether there is a clear genetic specificity for synthesis of these oligosaccharides, N-glycosides from two preparations of bovine fetuin, each from a single calf, were examined. Both of these structures were present in each calf, and there was only a subtle quantitative difference in the ratio of these two structures between the calves. Thus, a specific galactosyltransferase, presumably required for the biosynthesis of the Gal4,4,3TRI structure, may exist in both of these individual calves. Comparison of fetuin N-glycosides was also extended to sheep, pig, and human alpha 2-HS-glycoprotein, the human counterpart of bovine fetuin, using high-pH anion-exchange chromatography of the reducing oligosaccharides as well as HPLC of their pyridinylamino derivatives. The N-glycosides of ovine fetuin also have both Gal4,4,4TRI and Gal4,4,3TRI structures in a ratio similar to that of bovine fetuin. However, the major N-glycoside of porcine fetuin is of a fucosyl biantennary complex type structure (structure C below) and human alpha 2-HS-glycoprotein has an N-glycoside which is almost exclusively a nonfucosylated biantennary structure (structure D). This species-specific presence of N-glycosides of fetuins and comparison with N-glycosides of other glycoproteins suggest that the polypeptide sequence of a glycoprotein may affect its N-glycan structure by regulating the activity of specific glycosyltransferases. [formula: see text]
Details
- Title: Subtitle
- Comparison of N-glycosides of fetuins from different species and human alpha 2-HS-glycoprotein
- Creators
- Tetsuo Hayase - Department of Biology, Johns Hopkins University, Baltimore, MarylandKevin G RiceKatarzyna M DziegielewskaMark KuhlenschmidtThomas ReillyYuan Chuan Lee
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.31(20), pp.4915-4921
- DOI
- 10.1021/bi00135a024
- PMID
- 1375510
- NLM abbreviation
- Biochemistry
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Publisher
- United States
- Language
- English
- Date published
- 05/26/1992
- Academic Unit
- Pharmaceutical Sciences and Experimental Therapeutics; Craniofacial Anomalies Research Center; Medicinal and Natural Products Chemistry
- Record Identifier
- 9984065322302771
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