uridine diphosphate galactose
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ChemBioChem ◽  
2021 ◽  
Author(s):  
Reza Mahour ◽  
Ju Weon Lee ◽  
Pia Grimpe ◽  
Simon Boecker ◽  
Valerian Grote ◽  
...  

2021 ◽  
Vol 22 (5) ◽  
pp. 2261
Author(s):  
Zhongxin Liang ◽  
Hongrui Liang ◽  
Yizhan Guo ◽  
Dong Yang

Cyanidin 3-O-galactoside (Cy3Gal) is one of the most widespread anthocyanins that positively impacts the health of animals and humans. Since it is available from a wide range of natural sources, such as fruits (apples and berries in particular), substantial studies were performed to investigate its biosynthesis, chemical stability, natural occurrences and content, extraction methods, physiological functions, as well as potential applications. In this review, we focus on presenting the previous studies on the abovementioned aspects of Cy3Gal. As a conclusion, Cy3Gal shares a common biosynthesis pathway and analogous stability with other anthocyanins. Galactosyltransferase utilizing uridine diphosphate galactose (UDP-galactose) and cyanidin as substrates is unique for Cy3Gal biosynthesis. Extraction employing different methods reveals chokeberry as the most practical natural source for mass-production of this compound. The antioxidant properties and other health effects, including anti-inflammatory, anticancer, antidiabetic, anti-toxicity, cardiovascular, and nervous protective capacities, are highlighted in purified Cy3Gal and in its combination with other polyphenols. These unique properties of Cy3Gal are discussed and compared with other anthocyanins with related structure for an in-depth evaluation of its potential value as food additives or health supplement. Emphasis is laid on the description of its physiological functions confirmed via various approaches.


Processes ◽  
2019 ◽  
Vol 7 (4) ◽  
pp. 227 ◽  
Author(s):  
Sha Sha ◽  
Zhuangrong Huang ◽  
Cyrus Agarabi ◽  
Scott Lute ◽  
Kurt Brorson ◽  
...  

Monoclonal antibodies (mAbs) are commonly glycosylated and show varying levels of galactose attachment. A set of experiments in our work showed that the galactosylation level of mAbs was altered by the culture conditions of hybridoma cells. The uridine diphosphate galactose (UDP-Gal) is one of the substrates of galactosylation. Based on that, we proposed a two-step model to predict N-linked glycoform profiles by solely using extracellular metabolites from cell culture. At the first step, the flux level of UDP-Gal in each culture was estimated based on a computational flux balance analysis (FBA); its level was found to be linear with the galactosylation degree on mAbs. At the second step, the glycoform profiles especially for G0F (agalactosylated), G1F (monogalactosylated) and G2F (digalactosylated) were predicted by a kinetic model. The model outputs well matched with the experimental data. Our study demonstrated that the integrated mathematical approach combining FBA and kinetic model is a promising strategy to predict glycoform profiles for mAbs during cell culture processes.


2016 ◽  
Vol 94 (11) ◽  
pp. 1318-1326 ◽  
Author(s):  
Giovanna Pannuzzo ◽  
Adriana Carol Eleonora Graziano ◽  
Martina Pannuzzo ◽  
Marcelo Fabricio Masman ◽  
Rosanna Avola ◽  
...  

Author(s):  
Annet M. Bosch ◽  
Elaine Murphy

There are three known inherited disorders of galactose metabolism: classic galactosemia (galactose-1-phosphate uridyltransferase deficiency), galactokinase deficiency, and uridine diphosphate galactose 4-epimerase deficiency. Classic galactosemia presents in the newborn period with liver and renal impairment and failure to thrive. Acute symptoms resolve when lactose is excluded from the diet, but long-term complications are frequent and include neurocognitive and social difficulties, speech and language problems, motor problems, and premature ovarian insufficiency. Patients with galactokinase deficiency develop cataracts, while the clinical spectrum of uridine diphosphate galactose 4-epimerase deficiency is broad, from a benign condition to a severe disorder similar to classic galactosemia. All are autosomal recessive conditions. Diagnosis is by measurement of enzyme activity in erythrocytes, confirmed by mutation analysis of the specific genes, GALT, GALK, or GALE.


1999 ◽  
Vol 80 (4) ◽  
pp. 374-376 ◽  
Author(s):  
J H Walter ◽  
R E P Roberts ◽  
G T N Besley ◽  
J E Wraith ◽  
M A Cleary ◽  
...  

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