Qualitative and Quantitative Determination of Caseins with Reverse‐Phase and Anion‐Exchange HPLC

Strange, E.D.; Hekken, Diane Van; Thompson, M.P.

doi:10.1111/j.1365-2621.1991.tb04787.x

Cited by 22 publications

(11 citation statements)

References 14 publications

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“…Other PAGE techniques such as isoelectric focussing PAGE (Dannenberg and Kessler, 1986) and alkaline PAGE under native conditions (Hillier, 1976) have reported CVs of 2-6% for the determined concentrations of individual whey proteins. HPLC techniques have produced CVs, ranging from about 2 to 10% (Bobe et al, 1998b;Strange et al, 1991) whereas studies on capillary electrophoresis have reported CVs of about 2.5-4% for the determined concentrations of the individual milk proteins (de Jong et al, 1993). Overall, these comparisons of the variability of the determined concentrations of the milk proteins indicate that the microfluidic chip technique may be a viable alternative to the traditional SDS-PAGE method as well as HPLC and capillary electrophoresis techniques.…”

Section: Reproducibility Standard Curves and The Quantification Of Tmentioning

confidence: 90%

The use of “lab-on-a-chip” microfluidic SDS electrophoresis technology for the separation and quantification of milk proteins

Anema

2009

International Dairy Journal

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Section: Reproducibility Standard Curves and The Quantification Of Tmentioning

confidence: 90%

The use of “lab-on-a-chip” microfluidic SDS electrophoresis technology for the separation and quantification of milk proteins

Anema

2009

International Dairy Journal

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“…Reversed-phase HPLC separations of whole and modified caseins were determined on a 22-cm CS column as described by Strange et al (1991). Aseignmentato as1-or 8-casein were made on the basis of retention time and the relationships of the peaks to each other.…”

Section: Hplcmentioning

confidence: 99%

Chemical properties of thiolated and succinylated caseins

Strange¹,

Holsinger²,

Kleyn³

1993

J. Agric. Food Chem.

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Gelation of casein may be improved by introduction of functional groups that are both hydrophilic and capable of forming disulfide bonds. Thiolated whole caseins were prepared with S-acetylmercaptosuccinic anhydride at four concentrations to study chemical properties related to gelation. Succinylated samples were prepared for comparison. Degree of modification was determined by decrease in reactive lysine content. Urea-PAGE showed decreased positive charge for modified proteins as degree of modification increased. In addition, asi-and 0-casein bands remained while x-and as2-casein bands disappeared compared to whole native casein. SDS-PAGE without added mercaptoethanol indicated formation of intermolecular disulfide bonds in the thiolated derivatives. All modified caseins precipitated in the presence of Ca2+, but the concentration needed increased with degree of modification. Thiolated caseins were less soluble in the presence of high Ca2+ levels than succinylated or native caseins. Changes observed indicate successful introduction of groups that may enhance gelation.

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“…/J-Lg variant B, a-Lac, BSA and Lf each appeared as an unique peak. Cas was composed of four different molecules which were eluted in the order K-, 0CS2-, aSi-and jS-casein, as already described in similar chromatographic conditions by Visser (1991) and Strange (1991). The major caseins (i.e.…”

Section: Preparation Of Purified Milk Proteinsmentioning

confidence: 99%

Enzyme immunoassay of specific human IgE to purified cows’ milk allergens

Wal

Bernard

Yvon³

et al. 1995

Food and Agricultural Immunology

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An immunometric enzyme immunoassay for specific immunoglobulin E (IgE) against five purified cows' milk allergens, β-lactoglobuHn, α-lactalbumin, bovine serum albumin, lactoferrin and whole casein fraction, has been developed. Allergens were immobilized on microtitration plates. After incubations with sera from allergic patients, specific IgE bound to the plastic were detected using a monoclonal anti-human IgE antibody labelled with acetylcholinesterase. Quantitative determinations were made by comparison with a doseresponse curve obtained under the same conditions with standard total IgE. A quantification limit of 0.08 IU ml -1 can thus be obtained with a coefficient of variation of lower than 5%. This allows specific IgE determinations of clinical significance in sera from allergic patients at a dilution of at least 1/10 (i.e. in a few µl of serum) with good precision and reproducibility. The determinations of specific IgE in sera from 11 patients allergic to cows' milk showed an excellent correlation of this assay with clinical data.

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Qualitative and Quantitative Determination of Caseins with Reverse‐Phase and Anion‐Exchange HPLC

Cited by 22 publications

References 14 publications

The use of “lab-on-a-chip” microfluidic SDS electrophoresis technology for the separation and quantification of milk proteins

The use of “lab-on-a-chip” microfluidic SDS electrophoresis technology for the separation and quantification of milk proteins

Chemical properties of thiolated and succinylated caseins

Enzyme immunoassay of specific human IgE to purified cows’ milk allergens

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