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The binding of human milk lactoferrin to immunoglobulin A
Author(s) -
Watanabe Toshiteru,
Nagura Hiroshi,
Keiichi Watanabe,
Brown William R.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80246-x
Subject(s) - lactoferrin , antibody , chemistry , immunoglobulin g , food science , biochemistry , biology , immunology
It was recognized that in human milk some amounts of lactoferrin (LF) were naturally bound to secretory IgA (sIgA). Since not only secretory component (SC) but also LF was released from sIgA by disulfide bond cleavage, it is conceivable that LF is naturally bound to IgA as well as SC. An in vitro binding test to LF and IgA was performed and the binding was confirmed by the use of an IgA—Sepharose 4B affinity column.