This HTML5 document contains 50 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n16http://localhost/temp/predkladatel/
n15http://linked.opendata.cz/resource/domain/vavai/projekt/
n8http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n17http://linked.opendata.cz/ontology/domain/vavai/
n13http://linked.opendata.cz/resource/domain/vavai/zamer/
n10http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F60461373%3A22330%2F04%3A00014771%21RIV06-MSM-22330___/
shttp://schema.org/
n5http://linked.opendata.cz/ontology/domain/vavai/riv/
skoshttp://www.w3.org/2004/02/skos/core#
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n7http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n19http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n11http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n6http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n18http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n14http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n12http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00014771%21RIV06-MSM-22330___
rdf:type
skos:Concept n17:Vysledek
dcterms:description
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 the almost 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 above 908C, these c Imunosondy pro termálně indukované změny ve struktuře syrovátkových proteinů a jejich aplikace na analýzu tepelně zpracovaných mlék 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 the almost 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 above 908C, these c
dcterms:title
Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks Imunosondy pro termálně indukované změny ve struktuře syrovátkových proteinů a jejich aplikace na analýzu tepelně zpracovaných mlék
skos:prefLabel
Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks Imunosondy pro termálně indukované změny ve struktuře syrovátkových proteinů a jejich aplikace na analýzu tepelně zpracovaných mlék
skos:notation
RIV/60461373:22330/04:00014771!RIV06-MSM-22330___
n5:strany
77-91
n5:aktivita
n6:Z n6:P
n5:aktivity
P(OK 384), Z(MSM 223300004)
n5:cisloPeriodika
2
n5:dodaniDat
n12:2006
n5:domaciTvurceVysledku
n8:4819640 n8:9261818 n8:9046976 n8:8065462
n5:druhVysledku
n18:J
n5:duvernostUdaju
n19:S
n5:entitaPredkladatele
n10:predkladatel
n5:idSjednocenehoVysledku
567343
n5:idVysledku
RIV/60461373:22330/04:00014771
n5:jazykVysledku
n11:eng
n5:klicovaSlova
immunoprobes; whey protein
n5:klicoveSlovo
n7:whey%20protein n7:immunoprobes
n5:kodStatuVydavatele
CZ - Česká republika
n5:kontrolniKodProRIV
[B33679C63F68]
n5:nazevZdroje
Food and Agricultural Immunology
n5:obor
n14:CE
n5:pocetDomacichTvurcuVysledku
4
n5:pocetTvurcuVysledku
6
n5:projekt
n15:OK%20384
n5:rokUplatneniVysledku
n12:2004
n5:svazekPeriodika
15
n5:tvurceVysledku
Mills, Clare E.N. Fukal, Ladislav Morgan, Michael R. A. Rauch, Pavel Kodíček, Milan Karamonová, Ludmila
n5:zamer
n13:MSM%20223300004
s:issn
0954-0105
s:numberOfPages
15
n16:organizacniJednotka
22330