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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 25 (1995), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Extensively hydrolysed protein formulas are widely used as an alternative diet for children with cow's milk allergy. Partially hydrolysed protein formulas have been noted in some studies as useful in the prevention of allergy in infants at high risk of atopy. Although normally well tolerated, these ‘hypoallergenic’ products have been reported to cause serious immunological reactions in very sensitive subjects.Objective Starting from these considerations, we studied some commercial hydrolysed formulas in search of biological data supporting the observed clinical reactions.Methods We set up an electrophoretic method sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) which allowed us to study the molecular weight of peptides contained in hydrolysed products. Then, using the immunoblotting technique we evaluated the reactivity of circulating IgE (from serum of children allergic to cow's milk proteins) with the residual intact proteins and with the peptides present in these formulas.Results Both group of milk proteins (caseins and whey proteins) were important allergens for children included in this study. The presence of high-molecular polypeptides was shown in partial hydrolysed formulas as such and in extensive hydrolysed products after protein enrichment by trichloroacetic acid (TCA) precipitation. Intact residual proteins were mainly responsible for the formation of FgE-antigen complexes observed in immunoblotting. More rarely, polypeptides of partial hydrolysed formulas were involved in immunological responses.Conclusions Both partial and extensive hydrolysed formulas could induce clinical reactions in very sensitive subjects. These responses are mainly associated with allergy to the small amounts of residual intact proteins.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Hydrolysed casein and whey protein formulas have been developed with the aim of preventing sensitization in infants at high risk of cow milk allergy. Subsequently these products have also been used tor treatment of children with cow milk allergy. However, severe reactions have occurred in some allergic infants led with these formulas raising doubts about their absolute safety and suggest the need for developing in vitro techniques for detection of eventual residual allergenic activity in such preparations.Objectives Our purpose was to evaluate the usefulness of monoclonal and polyclonal antibodies against casein components (αβ and κ casein) as reagents for the detection of the residual antigenic activity of casein components in several hydrolysed formulas.Methods The monoclonal and polyclonal antibodies were produced according to standard procedures by immunizing female Balb/c mice with casein fraction (a mixture of α, β and κ casein). ELISA assays were developed to test the specificity of the antibodies and to detect and evaluate the amount of residual antigenic activity of the casein components in hydrolysed formulas.Results Use of polyclonal antiserum specific for casein allowed detection of residual antigenic activity of casein components in all partial hydrolysates and in the two extensive whey protein hydrolysates in the amounts ranging from 0.05 to 0.67% of total protein. No such activity was detectable in either the two extensive casein hydrolysates tested or the aminoacid based formula. The polyclonal antiserum proved to be more suitable than monoclonals for detecting residual antigenic activity in the hydrolysates. The monoclonal antibodies were directed against epitopes expressed on different casein components.Conclusions In this study the ELISA inhibition assay with polyclonal antibodies specific for casein components of cow milk proved to be a sensitive method for estimating residual antigenicity in the hydrolysed formulas commercially available for infants with cow milk allergy suggesting their potential application for the quality control of hypoallergenic infant formulas.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Partial and extensive hydrolysed protein formulae have been developed to lower or eliminate the antigenicity of milk proteins. Although normally well tolerated, extensive hydrolysutes have been reported to induce serious allergic reactions in very sensitive children. Moreover, clinical praetice has often raised concern about the role of partial hydrolysates in cow's milk allergy prevention.Objective Starting from these considerations, we used anti-casein monoclonal antibodies to evaluate the presence of residual antigenic activity in both partially and extensively protein hydrolysates.Methods Electrophoretic analyses associated with immunoblotting technique were performed using nine protein-enriched commercial formulae.Results The presence of different amounts of residual intact cow's milk proteins and/or polypeptidic material with conserved antigenic activity (according to the extensive or partial hydrolysis) was verified in most milk-based samples considered.Conclusion The use of monoclonal antibodies and immunoblotting could be useful for the quality control of commercial hypoaliergenic' formulae.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Little information is available on the reaction products of formaldehyde (FA) with milk components. An isoelectric focusing (IEF) method was developed which detected a unique protein band with pi = 6.7 in defatted Grana Padano cheese samples prepared with FA. The quantity of FA (ppm) added to milk may be extrapolated by calculating the amount of protein associated with this band. The IEF method was rapid, simple, highly specifiC., sensitive, reproducible, inexpensive and easy to utilized in routine controls.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This paper describes the chemical characterization of cocoa hulls, a potential source of high-methoxyl pectins (HMP). The content of some antinutritive compounds and potentially toxic compounds is also reported. Use of 2-propanol is proposed for the preliminary clean-up of the hulls and for the washing of the gel. Antinutritive and potentially toxic compounds seem not to limit the use of cocoa hulls. Lindane and ochratoxin A were easily removed together with fat using 2-propanol during preliminary clean up. The pectins (partially purified, yield: 1.29 ± 0.08%) showed a high methoxylation degree (%DE) of 60.53 ± 6.09%, and a viscosity of 16,200 cPs (5 rpm 20 °C). Washing procedures permit the decrease of the gel acidity from pH 1.97 to pH 3.76.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Allergy 60 (2005), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Allergy 60 (2005), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Objective:  This review provides updated information on conformational and sequential epitopes identified in bovine serum albumin (BSA) and summarizes available data about the role of structural modifications on BSA antigenicity/allergenicity.Data sources:  Data on beef allergy and BSA antigenicity are reported, with reference both to the basic literature and to clinical results obtained by our group.Results and discussion:  BSA is an important allergen involved in milk and beef allergy. The presence of conformational epitopes has been suggested by indirect evidence, while at least one sequential epitope has been experimentally identified. The role of structural modifications on BSA antigenicity is discussed as well as the increased tolerance observed in allergic subjects consuming beef as strained (homogenized) and freeze-dried derivatives.Conclusion:  Study of the molecular characteristics of a known major allergen allows the identification of technological processes that may be capable of improving the tolerance of allergic subjects to a specific food. Even though any hoped for reduced allergenicity must be verified under medical supervision, the use of new products could obviate the need to avoid important foods such as meat in childhood.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Allergy 53 (1998), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The effect of heat on the allergenicity of beef and bovine serum albumin was investigated among 10 toddlers skin prick test (SPT)-positive to raw and cooked beef. The meat-allergy diagnosis was confirmed during double-blind, placebo-controlled food challenge (DBPCFC) with 180 g of beef cooked for 5 min at 100°C. SPT with homogenized and freeze-dried beef, and heated and unheated bovine serum albumin were performed. Both heated and unheated bovine serum albumin, homogenized beef, and freeze-dried beef were used in trial DBPCFC. All children were SPT-positive to unheated bovine serum albumin. Seven were positive to heated bovine serum albumin, one to freeze-dried beef, and none to homogenized beef. DBPCFCs were negative for homogenized beef and freeze-dried beef, positive for unheated bovine serum albumin in five patients, and positive for heated albumin in four children. We conclude that heating reduces sensitization to beef and bovine serum albumin but does not abolish reactivity to albumin under home conditions. However, industrially heat-treated and sterilized homogenized beef and freeze-dried beef may be suitable substitutes in beef-allergic children's diets.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Phytochemistry 20 (1981), S. 2071-2075 
    ISSN: 0031-9422
    Keywords: Leguminosae ; Lupinus albus ; glycoproteins ; seed amino acids. ; seed proteins ; white lupine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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