Zobrazeno 1 - 10
of 49
pro vyhledávání: '"John W. Holland"'
Publikováno v:
Milk Proteins
Milk Proteins. Elsevier
Milk Proteins. Elsevier
The caseins exhibit a high degree of heterogeneity as a result of posttranslational modifications (PTMs). Phosphorylation of the αs1-, αs2-, and β-caseins and glycosylation of κ-casein are the best-known modifications and are critical for the for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d713eb50c730a54fc21dc2879c377e9
https://doi.org/10.1016/b978-0-12-815251-5.00005-0
https://doi.org/10.1016/b978-0-12-815251-5.00005-0
Autor:
Skelte G. Anema, Alan Baldwin, Sarah Berry, Etske Bijl, Mike Boland, Thérèse Considine, Stephen Davis, Hilton C. Deeth, Matthew Digby, Didier Dupont, Patrick J.B. Edwards, Ashling Ellis, John Flanagan, P.F. Fox, Kelvin K.T. Goh, D.A. Goulding, Chad Harland, W. James Harper, Sheelagh A. Hewitt, Kerianne Higgs, Jeremy Hill, John W. Holland, David S. Horne, Lee M. Huffman, Thom Huppertz, Geoffrey B. Jameson, Christophe Lefèvre, Simon M. Loveday, John A. Lucey, Karensa Menzies, Paul J. Moughan, Kevin R. Nicholas, J.A. O’Mahony, Sally D. Poppitt, Debashree Roy, Anwesha Sarkar, Pierre Schuck, Julie Sharp, Paul Sheehy, Pranav K. Singh, Harjinder Singh, Russell Snell, Anges Teo, Daniel Tomé, Peter Williamson, Aiqian Ye
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::810bb4c6bcf380efecf9876d2cf1189e
https://doi.org/10.1016/b978-0-12-815251-5.09990-4
https://doi.org/10.1016/b978-0-12-815251-5.09990-4
Publikováno v:
Food Chemistry. 141:1203-1210
Lactosylation in stored milk powder was quantified by multiple reaction monitoring (MRM), a mass spectrometry-based quantification method. The MRM method was developed from a knowledge of peptide fragmentation. The neutral losses of 162 Da (cleavage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2ee3150242312e585eff3f52634710f
https://doi.org/10.1016/j.foodchem.2013.03.073
https://doi.org/10.1016/j.foodchem.2013.03.073
Publikováno v:
International Dairy Journal. 31:83-91
Protein cross-linking, a possible cause of loss of solubility of milk protein concentrate (MPC) powder, may occur via advanced Maillard reaction products (e.g., methylglyoxal) or dehydroalanine. This study was designed to determine the relevance of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f0b394669ba2a4ebde99d68eb71f1f9e
https://doi.org/10.1016/j.idairyj.2013.02.013
https://doi.org/10.1016/j.idairyj.2013.02.013
Publikováno v:
Food Chemistry
Milk proteins are susceptible to chemical changes during processing and storage. We used proteomic tools to analyse bovine αS1-casein in UHT milk. 2-D gels of freshly processed milk αS1-casein was presented as five or more spots due to genetic poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cee7ff41a5b4508aecd9ecaf81d624c1
https://doi.org/10.1016/j.foodchem.2012.01.070
https://doi.org/10.1016/j.foodchem.2012.01.070
Publikováno v:
Jensen, H B, Holland, J W, Poulsen, N A & Larsen, L B 2012, ' Milk protein genetic variants and isoforms identified in bovine milk representing extremes in coagulation properties ', Journal of Dairy Science, vol. 95, no. 6, pp. 2891-2903 . https://doi.org/10.3168/jds.2012-5346
A gel-based proteomic approach consisting of 2-dimensional gel electrophoresis coupled with mass spectrometry was applied for detailed protein characterization of a subset of individual milk samples with extreme rennet coagulation properties. A milk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5e9bd4511edf40ec15fec1625b8a948
https://doi.org/10.3168/jds.2012-5346
https://doi.org/10.3168/jds.2012-5346
Publikováno v:
Food Chemistry. 132:655-662
Milk proteins undergo chemical changes such as lactosylation, deamidation and protein cross-linking during processing and storage of milk products. A proteomic technique combining two-dimensional gel electrophoresis and mass spectrometry was used to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcd61ff1f0e7812816fa434aad7bf4de
https://doi.org/10.1016/j.foodchem.2011.11.012
https://doi.org/10.1016/j.foodchem.2011.11.012
Publikováno v:
Journal of Agricultural and Food Chemistry. 59:1837-1846
Molecular changes in milk proteins during storage of UHT-treated milk have been investigated using two-dimensional electrophoresis (2-DE) coupled to MALDI-TOF mass spectrometry. UHT-treated samples were stored at three different temperatures, 4 °C,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1dcaa1f7aba5e5c691987fc8c55933b
https://doi.org/10.1021/jf104395v
https://doi.org/10.1021/jf104395v
Publikováno v:
Journal of Proteome Research. 7:5017-5027
Mammalian breast milk contains an array of proteins and other nutrients essential for the development of the newborn. In human milk, the caseins (alpha S1, beta and kappa) are a major class of proteins; however, the dynamic range of concentrations in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e42b9837dc9ceec899febc362baad5b
https://doi.org/10.1021/pr800387s
https://doi.org/10.1021/pr800387s
Publikováno v:
PROTEOMICS. 5:990-1002
The ability of two-dimensional gel electrophoresis (2-DE) to separate glycoproteins was exploited to separate distinct glycoforms of kappa-casein that differed only in the number of O-glycans that were attached. To determine where the glycans were at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24f0aaea142af247676da75501aa1294
https://doi.org/10.1002/pmic.200401098
https://doi.org/10.1002/pmic.200401098