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Phosphorylation and...
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Sheng, BuleiAarhus University
(författare)
Phosphorylation and glycosylation isoforms of bovine κ-casein variant E in homozygous Swedish Red cow milk by liquid chromatography-electrospray ionization mass spectrometry
- Artikel/kapitelEngelska2022
Förlag, utgivningsår, omfång ...
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American Dairy Science Association,2022
Nummerbeteckningar
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LIBRIS-ID:oai:lup.lub.lu.se:67f1db68-9bba-4dbe-a501-927c435d86ac
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https://lup.lub.lu.se/record/67f1db68-9bba-4dbe-a501-927c435d86acURI
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https://doi.org/10.3168/jds.2021-21172DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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Ämneskategori:ref swepub-contenttype
Anmärkningar
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Variations in the phosphorylation and glycosylation patterns of the common κ-casein (CN) variants A and B have been explored, whereas studies on variant E heterogeneity are scarce. This study reports for the first time the detailed phosphorylation and glycosylation pattern of the κ-CN variant E in comparison with variants A and B. Individual cow milk samples representing κ-CN genotype EE (n = 12) were obtained from Swedish Red cows, and the natural posttranslational modifications of its κ-CN were identified and quantified by liquid chromatography-electrospray mass spectrometry. In total, 12 unique isoform masses of κ-CN variant E were identified. In comparison, AA and BB milk consisted of 14 and 17 unique isoform masses, respectively. The most abundant κ-CN E isoform detected in the EE milk was the monophosphorylated, unglycosylated [1P 0G, ∼70%; where P indicates phosphorylation from single to triple phosphorylation (1–3P), and G indicates glycosylation from single to triple glycosylation (1–3G)] form, followed by diphosphorylated, unglycosylated (2P 0G, ∼12%) form, resembling known patterns from variants A and B. However, a clear distinction was the presence of the rare triphosphorylated, nonglycosylated (3P 0G, ∼0.05%) κ-CN isoform in the EE milk. All isoforms detected in variant E were phosphorylated, giving a phosphorylation degree of 100%. This is comparable with the phosphorylation degree of variants A and B, being also almost 100%, though with very small amounts of nonphosphorylated, glycosylated isoforms detected. The glycosylation degree of variant E was found to be around 17%, a bit higher than observed for variant B (around 14%), and higher than variant A (around 7%). Among glycosylation, the glycan e was the most common type identified for all 3 variants, followed by c/d (straight and branched chain trisaccharides, respectively), and b. In contrast to κ-CN variants A and B, no glycan of type a was found in variant E. Taken together, this study shows that the posttranslational modification pattern of variant E resembles that of known variants to a large extent, but with subtle differences.
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Biuppslag (personer, institutioner, konferenser, titlar ...)
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Thesbjerg, Martin N.Aarhus University
(författare)
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Glantz, MariaLund University,Lunds universitet,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)food-mgn
(författare)
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Paulsson, MarieLund University,Lunds universitet,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)ltkk-mpa
(författare)
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Nielsen, Søren D.Aarhus University
(författare)
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Poulsen, Nina A.Aarhus University
(författare)
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Larsen, Lotte B.Aarhus University
(författare)
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Aarhus UniversityAvdelningen för livsmedel och läkemedel
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Journal of Dairy Science: American Dairy Science Association105:3, s. 1959-19650022-0302
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