"Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks" . "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"@en . "RIV/60461373:22330/04:00014771!RIV06-MSM-22330___" . . . "Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks" . . "15"^^ . "Imunosondy pro term\u00E1ln\u011B indukovan\u00E9 zm\u011Bny ve struktu\u0159e syrov\u00E1tkov\u00FDch protein\u016F a jejich aplikace na anal\u00FDzu tepeln\u011B zpracovan\u00FDch ml\u00E9k"@cs . . "Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks"@en . "Mills, Clare E.N." . "Fukal, Ladislav" . "[B33679C63F68]" . "Morgan, Michael R. A." . . . "RIV/60461373:22330/04:00014771" . "567343" . "77-91" . "Rauch, Pavel" . . "6"^^ . . "P(OK 384), Z(MSM 223300004)" . "Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks"@en . . . "22330" . "immunoprobes; whey protein"@en . "15" . . "4"^^ . "0954-0105" . . "Kod\u00ED\u010Dek, Milan" . "Imunosondy pro term\u00E1ln\u011B indukovan\u00E9 zm\u011Bny ve struktu\u0159e syrov\u00E1tkov\u00FDch protein\u016F a jejich aplikace na anal\u00FDzu tepeln\u011B zpracovan\u00FDch ml\u00E9k"@cs . "Karamonov\u00E1, Ludmila" . . . "Imunosondy pro term\u00E1ln\u011B indukovan\u00E9 zm\u011Bny ve struktu\u0159e syrov\u00E1tkov\u00FDch protein\u016F a jejich aplikace na anal\u00FDzu tepeln\u011B zpracovan\u00FDch ml\u00E9k"@cs . "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" . . "2" . . . "Food and Agricultural Immunology" . . "CZ - \u010Cesk\u00E1 republika" . .