Two‐dimensional gel electrophoresis/matrix‐assisted laser desorption/ionisation mass spectrometry of commercial bovine milk

Galvani, Marina; Hamdan, Mahmoud; Righetti, Pier Giorgio

doi:10.1002/rcm.220

Cited by 52 publications

(42 citation statements)

References 16 publications

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“…Proteolysis products of bCN are detected and identified as protein spots ranging from 9 kDa (Galvani et al, 2001) to just a few residues short of the mass of the intact protein (Galvani et al, 2000(Galvani et al, , 2001Yamada et al, 2002;Murakami et al, 1998). Other significant proteolysis products of casein detectable by 2D-PAGE include para-kCN, the product of kCN digestion with rennin (Goldfarb, 1999).…”

Section: Proteolysismentioning

confidence: 99%

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Milk proteomics

O’Donnell

Holland

Deeth

et al. 2004

International Dairy Journal

130

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Milk proteins have been studied continuously for over 50 years. Knowledge of this complex protein system has evolved incrementally in recent decades, largely coinciding with advances in technology. Proteomics and associated technologies have the potential to facilitate further advances in our knowledge of milk proteins. Proteomics allows for the detection, identification and characterization of milk proteins. More importantly, proteomics facilitates the analysis of large numbers of milk proteins simultaneously.In the first part of this review we provide a description of the key techniques used within proteomic methodologies, with an emphasis on their general uses within proteomics. In the second part we summarize recent applications of proteomics to milk proteins and highlight the potential for new and rapid advances in the analysis of milk proteins. In particular, we emphasise the effectiveness of two-dimensional gel electrophoresis in combination with various mass spectrometry techniques for the detailed characterization of milk proteins. r

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Section: Proteolysismentioning

confidence: 99%

“…Galvani et al (2000),2 Galvani et al (2001),3 Marvin et al (2002),4 Roncada et al (2002),5 Quaranta et al (2001),6 Yamada et al (2002),7 Murakami et al (1998),8 Baeker et al (2002). a B=bovine; H=human; C=caprine.…”

unclassified

Milk proteomics

O’Donnell

Holland

Deeth

et al. 2004

International Dairy Journal

130

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show abstract

“…Galvani, Hamdan, and Righetti (2001) separated the proteins in commercial bovine milk with this technique using two different pH gradients, 3-10 and 6-11; the latter range gave better spot resolution for separation of the basic proteins. The molecular masses of the proteins were determined by using MALDI-TOF-MS. Their study draws attention to the difficulty in identifying basic proteins with low molecular weight (o12 kDa) commonly encountered in milk samples.…”

Section: Introductionmentioning

confidence: 99%

Two-dimensional gel electrophoresis of proteins and peptides in bovine milk

Lindmark-Månsson¹,

Timgren

Aldén³

et al. 2005

International Dairy Journal

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“…The proteome is a complete set of translated proteins in a given biological sample (O'Donnell et al, 2004). Proteomics have been used to investigate bovine milk protein fractions either CN (Galvani et al, 2001), major whey components (Galvani et al, 2001), low abundance proteins (Yamada et al, 2002) or milk fat globule membrane proteins (Reinhardt and Lippolis, 2006). Further, phosphorylation and glycosylation of bovine κ-CN have also been characterized by Holland et al (2006).…”

Section: Introductionmentioning

confidence: 99%

Effects of the processing methods of corn grain and soybean meal on milk protein expression profiles in dairy cows

Shen

Liu

2015

Animal

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A proteomic approach was used to investigate the effects of the processing method of corn grain and soybean meal on the milk protein expression profile in lactating dairy cows. A total of 12 multiparous Holstein dairy cows were used in a 4 × 4 Latin square design with a 2 × 2 factorial arrangement. The primary factors examined were corn (finely ground (FGC) v. steam-flaked (SFC)) and soybean meal (solvent-extracted (SSBM) v. heat-treated (HSBM)), which were used to formulate four diets with the same basal ingredient: 27% FGC and 9% SSBM; 27% SFC and 9% SSBM; 27% FGC and 9% HSBM; and 27% SFC and 9% HSBM. Each period lasted for 21 days. Milk samples were collected on days 18, 19 and 20 of each period. Changes in the milk proteins were assessed by two-dimensional (2D) electrophoresis and ImageMaster 2D Platinum 6.0 software. A total of 13 spots displayed variations in protein spot abundance according to the statistical analysis. These spots were identified by a matrix-assisted laser desorption/ ionization-time of flight/time of flight MS. According to the gels, the relative abundance of α s2 -casein (CN) fragments was higher in the cows fed the SFC-HSBM than that for SFC-SSBM, whereas β-CN, α-lactalbumin and zinc-alpha-2-glycoprotein fragments were down-regulated in HSBM-fed cows. The relative decrease of β-CN expression was validated by western blot and agreed with the MS data. These results suggested that the method used to process soybean meal modified the synthesis and secretion of milk proteins in lactating dairy cows' mammary glands.

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Two‐dimensional gel electrophoresis/matrix‐assisted laser desorption/ionisation mass spectrometry of commercial bovine milk

Cited by 52 publications

References 16 publications

Milk proteomics

Milk proteomics

Two-dimensional gel electrophoresis of proteins and peptides in bovine milk

Effects of the processing methods of corn grain and soybean meal on milk protein expression profiles in dairy cows

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