Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ming-Chuan Shao"'
Publikováno v:
Carbohydrate Research. 251:163-173
The specificity of Golgi-membrane glycoprotein 6-α-[ l -fucosyltransferase [GDP-[ l ]-fucose: 2-acetamido-2-deoxy-β-[ d ]-glucoside (Fuc → Asn-linked GlcNAc) 6-α-[ l ]-fucosyltransferase; EC 2.4.1.68] has been assessed with regard to substrate c
Publikováno v:
Journal of Biological Chemistry. 266:4810-4815
Sugar-binding characteristics of rat serum mannose-binding protein (MBP) were studied using the carbohydrate-recognition domain of this protein expressed from a cloned cDNA. To assess the binding affinity of various test compounds, they were added as
Autor:
F. Wold, S. H. Hixson, Ming-Chuan Shao, George A. Krudy, A. Flores-Carreon, Arnold D. Gomez, Paul R. Rosevear
Publikováno v:
Journal of Biological Chemistry. 265:754-759
When a derivatized oligosaccharide isolated from ovalbumin and containing 6 mannose residues was incubated with yeast membranes and GDP-mannose, two sets of products were obtained, a high molecular weight one containing about 25 mannose residues and
Autor:
Christopher C.Q. Chin, Ming-Chuan Shao
Publisher Summary Streptavidin–biotinylglycopeptide–lectin complexes can be used in the detection of glycopeptides and the determination of lectin specificity at the picomole level. The method is based on the high affinity between streptavidin an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a698c89acb63f33ad566b929f2595b5d
https://doi.org/10.1016/s0076-6879(94)47020-0
https://doi.org/10.1016/s0076-6879(94)47020-0
Autor:
Christopher C.Q. Chin, Ming-Chuan Shao
Publikováno v:
Analytical biochemistry. 207(1)
Glycopeptide-containing fractions in HPLC peptide maps can be detected by a simple application of the microtiter plate-bound streptavidin-biotinylated glycopeptide-lectin method ( M.-C. Shao, 1992 , Anal. Biochem. , 205, 77–82). To illustrate this
Publisher Summary Biotinylated glycans bound to avidin or streptavidin represent useful glycoprotein models for the study of both glycan processing by Golgi enzymes and glycoprotein interactions with lectins/receptors. The radiolabeled derivative wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2abe5e8118c749f151bb457c6796efa
https://doi.org/10.1016/0076-6879(90)84331-a
https://doi.org/10.1016/0076-6879(90)84331-a
Autor:
Ming-Chuan Shao, F. Wold
Publikováno v:
Journal of Biological Chemistry. 264:6245-6251
Using the avidin-biotinyl glycan system reported previously (Shao, M.-C., and Wold, F. (1987) J. Biol. Chem. 267, 2968-2972), we have compared the processing efficiency of oviduct enzymes acting on different glycan-(biotinyl)Asn and glycan-(6-biotina
Autor:
F. Wold, Ming-Chuan Shao
Publikováno v:
Journal of Biological Chemistry. 262:2968-2972
In an attempt to evaluate the effects of the protein matrix on the specificity of glycoprotein processing in Golgi membranes, we have developed a model neoglycoprotein consisting of biotinylated glycans bound noncovalently to avidin (Chen, V. J., and
Publikováno v:
The FASEB Journal. 2:2819-2824
Ion exchange chromatography at high pH with pulsed amperometric detection of the eluted glycans permitted resolution of the eight major components in the mixture of asparagine-linked glycans derived from the single glycosylation site of ovalbumin. Th