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Human milk components cross‐reacting with antibodies against bovine β‐lactoglobulin
Author(s) -
Neuteboom B,
Giuffrida MG,
Cantisani A,
Napolitano L,
Alessandri A,
Fabris C,
Bertino E,
Conti A
Publication year - 1992
Publication title -
acta pædiatrica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 115
eISSN - 1651-2227
pISSN - 0803-5253
DOI - 10.1111/j.1651-2227.1992.tb12276.x
Subject(s) - antiserum , beta lactoglobulin , bovine milk , coomassie brilliant blue , casein , antibody , whey protein , epitope , chromatography , microbiology and biotechnology , beta (programming language) , biochemistry , medicine , biology , chemistry , staining , immunology , pathology , computer science , programming language
The human whey components cross‐reacting with antibodies raised against bovine and/or equine β‐lactoglobulin were screened systematically. The milk of six women on a normal diet was collected within 72 h of confinement and whey components were fractionated by high‐speed size exclusion chromatography and reversed‐phase techniques. The fractions which were immunoreactive in double diffusion experiments with antisera anti‐bovine and/or equine β‐lactoglobulin were subsequently purified by native PAGE and then electroblotted on Pro‐blott membrane (Western blotting). Pro‐blot membranes were stained in parallel with Coomassie and by immunostaining using antibodies against bovine and/or equine β‐lactoglobulin as first antibody solution. The immunoreactive bands were cut out from the membrane and N‐terminally sequenced; all the immunoreactive components were clearly identified as human β‐casein or its (mainly tryptic) fragments. The strong antigenic similarity between human β‐casein and β‐lactoglobulin (bovine and equine) might be of immunological importance; it could mean that breast‐fed neonates risk being sensitized to β‐lactoglobulin irrespective of the presence of cow's milk in the mother's diet.