Analysis of beta-casein and its phosphoforms in human milk

Kroening, T A; Mukerji, Pradip; Hards, Robert G.

doi:10.1016/s0271-5317(98)00098-0

Cited by 20 publications

(13 citation statements)

References 23 publications

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“…Important changes in the absolute and relative β-CN and κ-CN concentrations of human milk were observed depending on the stage of lactation. As previously reported, especially for β-CN and for limited samplings, by some authors using other analytical methods (2,14,15), β-CN and κ-CN absolute concentrations and their relative percentages among total proteins increased from colostrum to transitional milk, then decreased at different rates from transitional to mature milk in which they became stable at least up to the end of the third month of lactation, thus supplying breast-fed infants with food intake for growth and development. Our results establish normal ranges (95% of the population) for β-CN (0.7-4.7 g/L) and for κ-CN (0.2-1.4 g/L) in healthy lactating mothers with wellestablished lactation.…”

Section: Discussionmentioning

confidence: 61%

“…Changes in both β-CN and κ-CN levels in human milk during lactation have not been much described, even if several methods (FPLC, polyacrylamide gel electrophoresis, isoelectric precipitation, or electroimmunodiffusion) have been proposed for the quantitation of these caseins, especially for β-CN (2,14,15). Microparticle-enhanced nephelometric immunoassays have been previously described as sensitive and accurate techniques for the determination of various human serum proteins (16) and of the main components of bovine milk, especially κ-CN (17) and β-CN (18).…”

Section: Introductionmentioning

confidence: 99%

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Changes in the ?-casein and ?-casein concentrations in human milk during lactation

Cuilli�re¹,

Tr�goat²,

B�n�³

et al. 1999

J. Clin. Lab. Anal.

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A microparticle-enhanced nephelometric immunoassay was developed for κ-casein quantification in human milk. Together with a previously reported β-casein comparable immunoassay, it was applied to 862 samples milk, collected from 82 mothers, to investigate the changes in casein concentrations in human milk during the first twelve weeks of lactation. κ-casein immunoassay is sensitive (detection limit in the reaction mixture, 0.02 mg/L) and can be performed in diluted milk, excluding any interference or sample pretreatment. It allowed the quantitation of κ-casein over a large range of concentrations (0.14-4.56 g/L) with accuracy and precision (coefficients of variation from 3 to 10%).βand κ-casein concentrations and percentages among milk total proteins increase between colostrum (2.6 g/L, 14.3% and 1.2 g/L, 6.5%, respectively) and transitional milk (4.4 g/L, 33.2% and 1.3 g/L, 9.5%), decrease at different rates from the third to the eighth week, then remain stable at least up to the end of the third month of lactation (2.7 g/L, 25.3% and 0.9 g/L, 8.5%). The β-casein/κ-casein ratio is higher in colostrum (0.61) than in transitional and mature milk (0.30) and could be related to a better digestibility of colostrum casein micelles by the neonate during the first days of life.

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Section: Discussionmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Changes in the ?-casein and ?-casein concentrations in human milk during lactation

Cuilli�re¹,

Tr�goat²,

B�n�³

et al. 1999

J. Clin. Lab. Anal.

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“…The analysis indicated a 69 % correlation among the four gels. On average, 210 spots were identified (SD = 18 spots), which is considered to be a good result in the fractionation of proteins by 2D-PAGE (Kroenig et al 1998). Spot 1 was also intense; this was the spot in which Hg was detected in the third dimension, which was the main objective of the fractionation of these proteins.…”

Section: Resultsmentioning

confidence: 92%

A Metalloproteomics Study on the Association of Mercury With Breast Milk in Samples From Lactating Women in the Amazon Region of Brazil

Santos

Cavecci

Vieira

et al. 2015

Arch Environ Contam Toxicol

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This study aimed to identify metalloproteins that lose their metal ions in the presence of mercury (Hg) and bind to Hg in breast milk samples collected from the riverine population of the Madeira River, a tributary of the Amazon River. Initially, total Hg was determined from the hair of lactating women to identify individuals who were contaminated followed by a proteomic analysis of breast milk samples through two-dimensional polyacrylamide gel electrophoresis after acetone precipitation. The presence of Hg in the obtained protein spots was determined by cold vapor atomic absorption spectrometry and cold vapor atomic fluorescence spectrometry. These determinations indicated the presence of Hg in one protein spot, which was then characterized through electrospray ionization tandem mass spectrometry. Based on searches in the UniProt database, this protein spot was identified as lysozyme C.

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“…Donkey beta-casein was identified in 19 of the 39 spots analyzed, by extensive peptide matching with horse beta-casein Q9GKK3, (Table 2) Some donkey beta-casein isoforms appear to be phosphorylated (spots 24, 30-32, 34, 36, Table 3), like the horse, human and bovine protein, or both phosphorylated and glycosylated, as a peculiar feature of DM (spots 13-19, Table 3) The presence of beta-casein in DM was already reported by Vincenzetti et al (23) after N-terminal sequencing identification, without reporting of any PTMs. As in HM, where beta-casein can account for up to 80% of the total caseins (30), beta-casein is also the predominant protein in DM.…”

Section: Beta-caseinmentioning

confidence: 99%

Detailed proteomic analysis on DM insight into its hypoallergenicity

et al. 2010

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Successful therapy in cow milk (CM) protein allergy rests upon completely eliminating CM proteins from the child's diet: it is thus necessary to provide a replacement food. Donkey milk (DM) has recently aroused scientific and clinical interest, above all among paediatric allergologists. A deeper knowledge of proteins in DM is necessary to evaluate the immunological and physiological properties of this natural substitute for cow's milk. The paper offers a detailed comparative analysis among the protein fractions of DM, CM and human milk, following an extensive proteomic study of the casein and whey proteins of DM performed by narrow pH range 2-DE. The detailed protein composition and structural features reported in this study provide insight into the molecular reasons for the hypoallergenicity of DM. Whole DM might constitute a valid substitute of CM in feeding children with CM protein allergy and it might also constitute the basis for formulas suitable for allergic subjects in the first year of life.

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Analysis of beta-casein and its phosphoforms in human milk

Cited by 20 publications

References 23 publications

Changes in the ?-casein and ?-casein concentrations in human milk during lactation

Changes in the ?-casein and ?-casein concentrations in human milk during lactation

A Metalloproteomics Study on the Association of Mercury With Breast Milk in Samples From Lactating Women in the Amazon Region of Brazil

Detailed proteomic analysis on DM insight into its hypoallergenicity

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