Nomenclature of the Proteins of Cows’ Milk—Sixth Revision

Farrell, Harold M.; Jiménez-Flores, Rafael; Bleck, Gregory T.; Brown, Eleanor M.; Butler, John E.; Creamer, Lawrence K.; Hicks, C.L.; Hollar, C.M.; Ng-Kwai-Hang, K.F.; Swaisgood, Harold E.

doi:10.3168/jds.s0022-0302(04)73319-6

Cited by 1,068 publications

(942 citation statements)

References 266 publications

(333 reference statements)

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“…Taking into account the calibration curve, it has been determined that the skimmed milk powder presents a native b-LG concentration of 12.77 6 0.58 mg/g and the UHT milk a concentration equal to 0.47 6 0.01 mg/mL. As compared to other references that mention the concentration of b-LG in raw milk [32,33], the concentrations that we have determined are lower. Now, it is well known that b-LG is highly sensitive to temperature [34].…”

Section: Quantification Of â-Lg In Milkmentioning

confidence: 48%

Capillary electrophoresis immunoassay using magnetic beads

Chen¹,

Busnel²,

Gassner³

et al. 2008

Electrophoresis

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Protein A-coated magnetic beads (0.3 mm) have been trapped in a small portion of a neutrally coated capillary (50 mm id). Anti-b-lactoglobulin (b-LG) antibodies have then been immobilized on the beads through strong affinity with protein A to subsequently capture b-LG from model or real samples. Once the immunocomplexes formed at physiological pH, a discontinuous buffer system has been used to release the partners and preconcentrate them by transient ITP. The antigens and antibodies have finally been separated by CZE and detected by UV absorbance. An LOQ of 55 nM has been achieved. This methodology has been applied to quantify native b-LG in pasteurized and ultra-high-temperature-treated bovine milk. All the described procedures, including immunosorbent preparation, sample extraction, cleanup, preconcentration, and separation are completely automated on a commercial CE instrument. As this CE immunoassay method is simple, rapid, selective, and sensitive, it should be a practical and attractive technology for the analysis of complicated biological samples.

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Section: Quantification Of â-Lg In Milkmentioning

confidence: 48%

Capillary electrophoresis immunoassay using magnetic beads

Chen¹,

Busnel²,

Gassner³

et al. 2008

Electrophoresis

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“…The bovine serum : colostrum IgG ratio is according to a previous publication. 35 The P-value of the statistical analysis (anova) is indicated.…”

Section: Discussionmentioning

confidence: 99%

Over‐expression of the bovine FcRn in the mammary gland results in increased IgG levels in both milk and serum of transgenic mice

Lü

Zhao

et al. 2007

Immunology

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SummaryThe neonatal Fc receptor (FcRn) protects immunoglobulin G (IgG) from catabolism and is also responsible for IgG absorption in the neonatal small intestine. However, whether it mediates the transfer of IgG from plasma to milk still remains speculative. In the present study, we have generated transgenic mice that over-express the bovine FcRn (bFcRn) in their lactating mammary glands. Significantly increased IgG levels were observed in the sera and milk from transgenic animals, suggesting that the over-expressed bFcRn could bind and protect endogenous mouse IgG and thus extend its lifespan. We also found that injected human IgG showed a significantly longer half-life (7-8 days) in the transgenic mice than in controls (2Á9 days). Altogether, the data suggested that bFcRn could bind both mouse and human IgG, showing a cross-species FcRnIgG binding activity. However, we found no selective accumulation of endogenous mouse IgG or injected bovine IgG in the milk of the transgenic females, supporting a previous hypothesis that IgG was transported from serum to milk in an inverse correlation to its binding affinity to FcRn.

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“…The four caseins represent 80% of cow milk proteins [2]. From one species to another, a large variability (quantitative as well as qualitative) is observed [3].…”

Section: Introductionmentioning

confidence: 99%

Translational efficiency of casein transcripts in the mammary tissue of lactating ruminants

Bevilacqua¹,

Helbling²,

Miranda³

et al. 2006

Reprod. Nutr. Dev.

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-Caseins are essentially concentrated in the colloidal fraction of ruminant milks as highly hydrated and mineralized spherical particles, termed casein micelles. They form a group of four peptide chains (α s1 , β, α s2 and κ), encoded by four structural genes (CSN1S1, CSN2, CSN1S2 and CSN3, respectively) of which the expression is regulated by lactogenic hormones. These phosphoproteins are synthesized, essentially during lactation, in the mammary epithelial cells and we show, for the first time, that their regulation is also controlled at the translational level. Apparently, the four casein messenger are not translated with the same efficiency. Specific amplification systems have been developed and optimized to quantify, by real time quantitative PCR (qPCR), transcripts encoding the four caseins starting from total RNA extracted from mammary tissues taken on goats (n = 4), ewes (n = 3) and cows (n = 3), in lactation. The relative proportions of each specific messenger (% of casein mRNA) were compared to the relative amounts of the corresponding caseins (% of whole casein) in milks sampled from the same animals, determined after fractionation by reverse phase HPLC and integration of the corresponding peak areas. From qPCR data, the four casein transcripts appeared to be present approximately at the same level of abundance (ca. 25%, except for defective genotypes at the CSN1S1 locus, in the goat) whereas the amounts of the corresponding proteins in milk were ranging between 9 and 38% of the whole casein fraction. A comparison of specific translational efficiencies (% of protein in milk/% of transcript in the mammary tissue), showed that α s1 -and β-casein transcripts are translated ca. 3-to 4-fold more efficiently than α s2 -and κ-casein transcripts. This seems to be the rule in the three ruminant species studied. More or less optimal contexts for initiation of translation (Kozak recognition sequence of the start codon) as well as 3' untranslated region (UTR) sequences and length might explain, at least in part, our results. These preliminary results which have now to be confirmed with a larger number of individuals to strengthen our findings and conclusions, provides, however, a rational explanation to the unbalanced casein distribution (approximate proportions 4:1:4:1 for α s1 :α s2 :β:κ, respectively) reported for ruminant milks. The possible effects of specific secondary structures in the 5' and 3' UTRs of casein messengers still have to be considered. milk / casein / mRNA / quantification / untranslated regions (UTRs) / RP-HPLC / real time quantitative PCR / goat / cow / ewe

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Nomenclature of the Proteins of Cows’ Milk—Sixth Revision

Cited by 1,068 publications

References 266 publications

Capillary electrophoresis immunoassay using magnetic beads

Capillary electrophoresis immunoassay using magnetic beads

Over‐expression of the bovine FcRn in the mammary gland results in increased IgG levels in both milk and serum of transgenic mice

Translational efficiency of casein transcripts in the mammary tissue of lactating ruminants

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