Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6-7
pubmed:dateCreated
1992-10-29
pubmed:abstractText
The human whey components cross-reacting with antibodies raised against bovine and/or equine beta-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 beta-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 beta-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 beta-casein or its (mainly tryptic) fragments. The strong antigenic similarity between human beta-casein and beta-lactoglobulin (bovine and equine) might be of immunological importance; it could mean that breast-fed neonates risk being sensitized to beta-lactoglobulin irrespective of the presence of cow's milk in the mother's diet.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0803-5253
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
469-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Human milk components cross-reacting with antibodies against bovine beta-lactoglobulin.
pubmed:affiliation
Centro Studio Alimentazione Animali del CNR Torino, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't