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Casein‐hydrolyzing activity of sIgA antibodies from human milk
Author(s) -
Odintsova Elena S.,
Buneva Valenti.,
Nevinsky Georgy A.
Publication year - 2005
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.743
Subject(s) - proteases , casein , biochemistry , polyclonal antibodies , chemistry , serine , protease , proteolytic enzymes , antibody , proteolysis , lactation , enzyme , microbiology and biotechnology , biology , immunology , pregnancy , genetics
During pregnancy and immediately after delivery (i.e. at the beginning of lactation), the female organism is frequently characterized by an immune status similar to that of patients with autoimmune diseases. In addition, lactation is associated with an appearance of catalytically active antibodies or abzymes (Abzs) with DNAse, RNase, ATPase, amylolitic, protein kinase and lipid kinase activities in breast milk. However, until now there were no examples of human milk Abzs with a proteolytic activity. We present the first evidence that electrophoretically and immunologically homogeneous human milk sIgAs possess a β‐casein‐hydrolyzing activity different from known proteases. Abzs specifically hydrolyze both human and bovine β‐caseins but not many other proteins tested. Using different methods including in situ analysis of proteolytic activity in a gel after SDS–PAGE it was shown that the observed proteolytic activity is an intrinsic property of human milk polyclonal sIgAs. Specific inhibitors of acidic and thiol proteases demonstrated a weak effect on proteolytic activity of Abzs, while a specific inhibitor of serine proteases (AEBSF) significantly inhibited the proteolytic activity of the abzymes. The K M value for human casein as a substrate was estimated (7.3 µ M ). Our findings suggest that the immune system of clinically healthy mothers can generate IgAs with a β‐casein‐specific serine protease‐like activity. Copyright © 2005 John Wiley & Sons, Ltd.