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Assays for Evaluati...
Assays for Evaluation of Substrates for and Inhibitors of β-1,4-Galactosyltransferase 7
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- Tykesson, Emil (författare)
- Lund University,Lunds universitet,Lungbiologi,Forskargrupper vid Lunds universitet,Lung Biology,Lund University Research Groups
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- Persson, Andrea (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för laboratoriemedicin,Department of Laboratory Medicine,Sahlgrenska Academy
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- Mani, Katrin (författare)
- Lund University,Lunds universitet,Glykobiologigruppen,Forskargrupper vid Lunds universitet,LUCC: Lunds universitets cancercentrum,Övriga starka forskningsmiljöer,Glycobiology,Lund University Research Groups,LUCC: Lund University Cancer Centre,Other Strong Research Environments
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- Ellervik, Ulf (författare)
- Lund University,Lunds universitet,Lungbiologi,Forskargrupper vid Lunds universitet,Centrum för analys och syntes,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Lung Biology,Lund University Research Groups,Centre for Analysis and Synthesis,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2021-10-10
- 2022
- Engelska.
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Ingår i: Glycosaminoglycans. Methods in Molecular Biology, vol 2303. Balagurunathan K., Nakato H., Desai U., Saijoh Y. (eds). - New York, NY : Springer. - 1064-3745 .- 1940-6029. - 9781071613986 ; , s. 477-486
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Abstract
Ämnesord
Stäng
- β-1,4-Galactosyltransferase 7 (β4GalT7) is a key enzyme in the synthesis of two classes of glycosaminoglycans (GAG), i.e., heparan sulfate (HS) and chondroitin/dermatan sulfate (CS/DS). GAG chains are linear polysaccharides of alternating hexuronic acid and N-acetylhexosamine residues, commonly linked to core proteins to form proteoglycans with important roles in the regulation of a range of biological processes. The biosynthesis of GAGs is initiated by xylosylation of a serine residue of the core protein followed by galactosylation, catalyzed by β4GalT7. The biosynthesis can also be initiated by xylosides carrying hydrophobic aglycons, such as 2-naphthyl β-D-xylopyranoside. We have cloned and expressed β4GalT7, and designed a cell-free assay to measure the activity of this enzyme. The assay employs a 96-well plate format for high throughput. In this chapter, we describe the cloning, expression, and purification of β4GalT7, as well as assays proposed for development of substrates for GAG priming and for investigating inhibitors of β4GalT7. © 2022, Springer Science+Business Media, LLC, part of Springer Nature.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Nyckelord
- Glycosaminoglycan biosynthesis
- Inhibitor
- Substrate
- Xylosides
- β-1
- 4-Galactosyltransferase 7
- β-1,4-Galactosyltransferase 7
Publikations- och innehållstyp
- vet (ämneskategori)
- kap (ämneskategori)
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