EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Reinvestigation of the carbohydrate chains of calf fetuin using carbon 13 nmr spectroscopy






Carbohydrate Research 152: 33-46

Reinvestigation of the carbohydrate chains of calf fetuin using carbon 13 nmr spectroscopy

The triantennary structure of the N-linked oligosaccharide side-chain of fetuin, elucidated by a combination of 13C-n.m.r. spectroscopy and enzymic degradations, accords with that reported earlier with respect to the branching pattern, but the ratio fo the N-acetylneuraminic acid linkages to galactose residues [.alpha.-(2 .fwdarw. 3) vs. .alpha.-(2 .fwdarw. 6)] was found to be 1:1, indicating structural heterogeneity of the side chains. Also one out of nine galactosyl residues is linked to 2- acetamido-2-deoxy-.beta.-D-glucose by a (1 .fwdarw. 3) rather tha a (1 .fwdarw. 4) linkage. The chemical shifts reported are in excellent agreement with those for the intact glycoprotein. Unusual chemical shift effects lead to the conclusion that the .alpha.-NeuAc-(2 .fwdarw. 6) residues interact with other parts of the oligosaccharide side-chain. The action of .beta.-D-galactosidase from Aspergillus niger on desialylated fetuin removed .apprx. 85% of the .beta.-Gal residues (1 .fwdarw. 4)-linked to GlcNAc and 65% of the .beta.-Gal residues (1 .fwdarw. 3)-linked to GalNAc, but none of the .beta.-Gal residues (1 .fwdarw. 3)-linked to GlcNAc.

(PDF 0-2 workdays service: $29.90)

Accession: 006292949



Related references

Reinvestigation of the carbohydrate chains of calf fetuin using 13C-n.m.r. spectroscopy. Carbohydrate Research 152: 33-46, 1986

One dimensional and two dimensional 905 megahertz carbon 13 nmr spectroscopy of the n linked triantennary oligosaccharide units of calf fetuin. S Letters: 257-260, 1986

Natural abundance carbon 13 nmr spectroscopy of 2 glyco asparagines derived from the core of n glycosidic carbohydrate chains. European Journal of Biochemistry 130(1): 111-116, 1983

One- and two-dimensional 90.5-MHz 13C-NMR spectroscopy of the N-linked triantennary oligosaccharide units of calf fetuin. Febs Letters 204(2): 257-260, 1986

Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin: indications for an a-N-acetylgalactosaminide a2-6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. The Journal of Biological Chemistry 258: 30-6, 1983

A two dimensional proton nmr 500 mhz and carbon 13 nmr 125 mhz study of n linked glycopeptides derived from calf fetuin. Carbohydrate Research 176(1): 1-16, 1988

Primary structure of the carbohydrate chain of soybean agglutinin. A reinvestigation by high resolution 1H NMR spectroscopy. Journal of Biological Chemistry 256(15): 7708-7711, 1981

Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. Journal of Biological Chemistry 258(12): 7430-7436, 1983

Primary structure of the carbohydrate chain of soybean agglutinin a reinvestigation by high resolution proton nmr spectroscopy. Journal of Biological Chemistry 256(15): 7708-7711, 1981

Biosynthesis of the o glycosidically linked oligo saccharide chains of fetuin indications for an alpha n acetyl galactosaminide alpha 2 6 sialyl transferase with a narrow acceptor specificity in fetal calf liver. Journal of Biological Chemistry 258(12): 7430-7436, 1983