Imunosondy pro termálně indukované změny ve struktuře syrovátkových proteinů a jejich aplikace na analýzu tepelně zpracovaných mlék

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012803" target="_blank" >RIV/60461373:22330/04:00012803 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/04:00014771

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks

Popis výsledku v původním jazyce

Polyclonal antisera have been raised to the whey proteins a-lactalbumin [a-La] and b-lactoglobulin [b-Lg], variants A and B. These antibody preparations have been used to develop enzyme-linked immunosorbent assays (ELISAs) for each of these proteins, which had limits of detection of 13 ng/ml [a-La], 27 ng/ml [b-Lg, variant A], and 20 ng/ml [b-Lg, variant B]. The a-La ELISA did not show any cross-reaction with b-Lg, and neither of the b-Lg ELISAs showed a cross-reactivity with a-La. However, despite thealmost identical sequences of variants A and B of b-Lg, the variant A ELISA had a cross-reactivity of 66% with variant B, whilst the variant B ELISA had a cross-reactivity of more than 200% with variant A. The effect of thermal treatment on the immunoreactivity of purified whey proteins was studied by ELISA and related to changes in secondary and tertiary structure determined using CD and fluorescence spectroscopy. The immunoreactivity of a-La determined by ELISA decreased on heating abo

Název v anglickém jazyce

Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks

Popis výsledku anglicky

Polyclonal antisera have been raised to the whey proteins a-lactalbumin [a-La] and b-lactoglobulin [b-Lg], variants A and B. These antibody preparations have been used to develop enzyme-linked immunosorbent assays (ELISAs) for each of these proteins, which had limits of detection of 13 ng/ml [a-La], 27 ng/ml [b-Lg, variant A], and 20 ng/ml [b-Lg, variant B]. The a-La ELISA did not show any cross-reaction with b-Lg, and neither of the b-Lg ELISAs showed a cross-reactivity with a-La. However, despite thealmost identical sequences of variants A and B of b-Lg, the variant A ELISA had a cross-reactivity of 66% with variant B, whilst the variant B ELISA had a cross-reactivity of more than 200% with variant A. The effect of thermal treatment on the immunoreactivity of purified whey proteins was studied by ELISA and related to changes in secondary and tertiary structure determined using CD and fluorescence spectroscopy. The immunoreactivity of a-La determined by ELISA decreased on heating abo

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/OK%20384" target="_blank" >OK 384: Rychlá specifická detekce Listerie monocytogenes pomocí protilátek</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Food and Agricultural Immunology

ISSN

0954-0105

e-ISSN

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Svazek periodika

15

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

15

Strana od-do

77-91

Kód UT WoS článku

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EID výsledku v databázi Scopus

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