N- and O-Glycosylation of a Commercial Bovine Whey Protein Product
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چکیده
منابع مشابه
O - Glycosylation Mimics N - Glycosylation in the 16 - kDa Fragment of Bovine
The NHz-terminal domain of pro-opiomelanocortin, designated as the 16-kDa fragment, is highly conserved throughout the vertebrate family and is likely therefore to have an important functional role. Bovine 16-kDa fragment is a 77residue glycopeptide, which has been found to be glycosylated at threonine 45 and asparagine 65. Available evidence suggests that glycoforms lacking glycans at the O-li...
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This review provides an overview on the methods available for analysis of O-glycosylation. Three major themes are addressed: analysis of released O-glycans including different O-glycan liberation, derivatization, and detection methods; analysis of formerly O-glycosylated peptides yielding information on O-glycan attachment sites; analysis of O-glycopeptides, representing by far the most informa...
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Background Genomic imprinting is a heritable and developmentally essential phenomenon by which gene expression occurs in an allele-specific manner1. While the imprinted alleles are primarily silenced by DNA methylation, it remains largely unknown how methylation is targeted to imprinting control region (ICR), also called differentially methylated region (DMR), and maintained. Here we show that ...
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Most secreted and cell membrane proteins in mammals are glycosylated. Many of these glycoproteins are also prevalent in milk and play key roles in the biomodulatory properties of milk and ultimately in determining milk's nutritional quality. Although a significant amount of information exists on the types and roles of free oligosaccharides in milk, very little is known about the glycans associa...
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ژورنال
عنوان ژورنال: Journal of Agricultural and Food Chemistry
سال: 2012
ISSN: 0021-8561,1520-5118
DOI: 10.1021/jf304000b