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Titolo:
Identification of the human beta-casein C-terminal fragments that specifically bind to purified antibodies to bovine beta-lactoglobnlin
Autore:
Conti, A; Giuffrida, MG; Napolitano, L; Quaranta, S; Bertino, E; Coscia, A; Costa, S; Fabris, C;
Indirizzi:
CNR, Ctr Studi Alimentaz Anim, I-10010 Colleretto Giacosa, TO, Italy CNR Colleretto Giacosa TO Italy I-10010 010 Colleretto Giacosa, TO, Italy Univ Turin, Cattedra Neonatol, Turin, Italy Univ Turin Turin ItalyUniv Turin, Cattedra Neonatol, Turin, Italy
Titolo Testata:
JOURNAL OF NUTRITIONAL BIOCHEMISTRY
fascicolo: 6, volume: 11, anno: 2000,
pagine: 332 - 337
SICI:
0955-2863(200006)11:6<332:IOTHBC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
COWS MILK ALLERGY; BREAST-FED INFANTS; PROTEIN; MOTHERS; PASSAGE;
Keywords:
human milk; allergy; cross-reactivity; maternal diet;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Conti, A CNR, Ctr Studi Alimentaz Anim, Bioind Pk Via Ribes 5, I-10010 Colleretto Giacosa, TO, Italy CNR Bioind Pk Via Ribes 5 Colleretto Giacosa TO Italy I-10010 aly
Citazione:
A. Conti et al., "Identification of the human beta-casein C-terminal fragments that specifically bind to purified antibodies to bovine beta-lactoglobnlin", J NUTR BIOC, 11(6), 2000, pp. 332-337

Abstract

The presence of foreign proteins in human milk after the ingestion of bovine dairy products is thought to be one of the possible causes of allergic sensitization in exclusively breast-fed predisposed infants. The immunologicdetermination of bovine beta-lactoglobulin (LC) concentration in human milk has been reported by several researchers, but the results are conflicting. Moreover, a strong cross-reactivity between antibodies to bovine beta-LG and human milk proteins and peptides was reported, throwing doubt on the reliability of radioimmunoassay and enzyme-linked immunosorbent assay detection and quantification assays for bovine beta-LG in human milk. Thus, the goal of this study was to isolate human milk peptides with a molecular mass greater than or equal to 1,000 Da cross-reactive with antibodies to bovine beta-LG in order to identify possible common epitopes between human and bovine milk proteins. The proteins were first isolated by affinity chromatography with purified polyclonal antibodies to bovine beta-LG, followed by gel filtration fast phase liquid chromatography and reverse phase-high performance liquid chromatography purification of the components specifically bound in the affinity separation step. Affinity-bound peptides were identified bydetermining their amino acid sequence. All the sequenced peptides belongedto the C-terminal part of human beta-casein, which confirms the cross-reactivity of human milk proteins and peptides with antibodies to bovine beta-LG and allows the identification of possible common epitopes between the twoproteins No bovine beta-LG peptides with a molecular mass greater than or equal to 1,000 Da were found in our milk samples from healthy mothers on a diet rich in bovine milk and dairy products. (J. Nutr. Biochem. 11:332-337,2000) (C) Elsevier Science Inc. 2000. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 17:50:43