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Characterization of Lactoferrin (LF) from Colostral Whey Using Anti‐LF Antibody Immunoaffinity Chromatography
Author(s) -
Tu Y.Y.,
Chen C.C.,
Chang JH.,
Chang HM.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb09442.x
Subject(s) - chemistry , colostrum , lactoferrin , chromatography , affinity chromatography , sepharose , whey protein , dissociation constant , antibody , biochemistry , receptor , biology , immunology , enzyme
Lactoferrin (LF) in colostral whey was isolated by anti‐LF immunoglobulin in yolk (IgY)‐Sepharose 4B immunoaffinity chromatography, and parameters such as binding capacity (q m ) and dissociation constant (K d , × 10 −6 M) of this immunoaffinity gel for LF were discussed. Purification folds for colostral whey I (from colostrum collected within 6 d of postpartum) and colostral whey II (from colostrum collected within 1 d of postpartum) by anti‐LF IgY‐immunoaffinity chromatography were 135.80 and 103.60, respectively. The recovery for LF in the same colostral whey sample by anti‐LF IgY‐immunoaffinity chromatography was 82 to 99 %. q m of anti‐LF IgY‐immunoaffinity gel for LF in colostral whey I and whey II were 0.372 and 0.272 mg LF/mL wet gel, respectively. K d of anti‐LF IgY‐immunoaffinity gel for LF in colostral whey I was 1.594 × 10 −6 M and II was 1.587 × 10 −6 M.