onr:"swepub:oai:DiVA.org:uu-52355"
Sökning: onr:"swepub:oai:DiVA.org:uu-52355" > Assessment of glyco...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03163naa a2200361 4500 | |
| 001 | oai:DiVA.org:uu-52355 | |
| 003 | SwePub | |
| 008 | 081017s1997 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-523552 URI |
| 040 | a (SwePub)uu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Lidholt, Kerstinu Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi4 aut0 (Swepub:uu)kerslid |
| 245 | 1 0 | a Assessment of glycosaminoglycan-protein linkage tetrasaccharides as acceptors for GalNAc- and GlcNAc-transferases from mouse mastocytoma. |
| 264 | 1 | c 1997 |
| 338 | a print2 rdacarrier | |
| 520 | a Two glycosaminoglycan-protein linkage tetrasaccharide-serine compounds, GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser and GlcA beta 1-3Gal(4-O-sulfate)beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, were tested as hexosamine accepters, using UDP-[H-3]GlcNAc and UDP-[H-3]GalNAc as sugar donors, and solubilized mouse mastocytoma microsomes as enzyme source. The nonsulfated Ser-tetrasaccharide was found to function as an acceptor for a GalNAc residue, whereas the Ser-tetrasaccharide containing a sulfated galactose unit was inactive. Characterization of the radio-labelled product by digestion with alpha-N-acetylgalactosaminidase and beta-N-acetylhexosaminidase revealed that the [H-3]GalNAc unit was alpha-linked, as in the product previously synthesized using serum enzymes, and not beta-linked as found in the chondroitin sulfate polymer. Heparan sulfate/heparin biosynthesis could not be primed by either of the two linkage Ser-tetrasaccharides, since no transfer of [H-3]GlcNAc from UDP-[H-3]GlcNAc could be detected. By contrast, transfer of a [H-3]GlcNAc unit to a [GlcA beta 1-4GlcNAca1-4](2)-GlcA beta 1-4-aMan hexasaccharide acceptor used to assay the GlcNAc transferase involved in chain elongation, was readily detected. These results are in agreement with the recent proposal that two different N-acetylglucosaminyl transferases catalyse the biosynthesis of heparan sulfate. Although the mastocytoma system contains both the heparan sulfate/heparin and chondroitin sulfate biosynthetic enzymes the Ser-tetrasaccharides do not seem to fulfil the requirements to serve as accepters for the first HexNAc transfer reactions involved in the formation of these polysaccharides. | |
| 653 | a Biosynthesis | |
| 653 | a GalNAc transferase | |
| 653 | a GlcNAc transferase | |
| 653 | a glycosaminoglycan | |
| 653 | a proteoglycan | |
| 700 | 1 | a Fjelstad, Mariau Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi4 aut |
| 700 | 1 | a Lindahl, Ulfu Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi4 aut |
| 700 | 1 | a Goto, F4 aut |
| 700 | 1 | a Ogawa, T4 aut |
| 700 | 1 | a Kitagawa, H4 aut |
| 700 | 1 | a Sugahara, K4 aut |
| 710 | 2 | a Uppsala universitetb Institutionen för medicinsk och fysiologisk kemi4 org |
| 773 | 0 | t Glycoconjugate Journalg 14:6, s. 737-742q 14:6<737-742x 0282-0080x 1573-4986 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-52355 |
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