Isolation of Immunoglobulin A (IgA) from Human Colostrum.
نویسندگان
چکیده
منابع مشابه
Site-specific glycosylation of secretory immunoglobulin A from human colostrum.
Secretory immunoglobulin A (sIgA) is a major glycoprotein in milk and plays a key role in mediating immune protection of the gut mucosa. Although it is a highly glycosylated protein, its site-specific glycosylation and associated glycan micro-heterogeneity have still not been fully elucidated. In this study, the site-specific glycosylation of sIgA isolated from human colostrum (n = 3) was analy...
متن کاملIsolation and characterization of a glycoprotein from human colostrum.
A glycoprotein was isolated from the M-1 acid glycoprotein fraction of human colostrum. It had a molecular weight of 31200 and contained 27% galactose, 21.7% hexosamine, 8.0% fucose and 10.8% sialic acid by weight. The glycoprotein had no absorption maxima in the 240-300nm region, and was virtually free of ABH(O) and M and N blood-group activity. Alkaline borohydride cleavage of the glycoprotei...
متن کاملPREPARATION OF ENRICHED IMMUNOGLOBULIN M AND IMMUNOGLOBULIN A FROM HUMAN PLASMA
As IgM and IgA-enriched preparations are needed to complete the immunotherapeutic spectrum, a simple procedure is described for the preparation of IgM and IgA enriched immunoglobulins. Fraction III which was prepared by cold ethanol fractionation was treated by octanoic acid followed by ethanol precipitation and ion-exchange chromatography using Sephadex DEAE A-50 and 0.1 M tris-D.35M NaCI ...
متن کاملPeptide mimetics of immunoglobulin A (IgA) and FcαRI block IgA‐induced human neutrophil activation and migration
The cross-linking of the IgA Fc receptor (FcαRI) by IgA induces release of the chemoattractant LTB4, thereby recruiting neutrophils in a positive feedback loop. IgA autoantibodies of patients with autoimmune blistering skin diseases therefore induce massive recruitment of neutrophils, resulting in severe tissue damage. To interfere with neutrophil mobilization and reduce disease morbidity, we d...
متن کاملBacterial agglutination studies with secretory IgA prepared from human gastrointestinal secretions and colostrum.
The function of human purified colostral and gastrointestinal IgA has been studied by its ability to agglutinate common gastrointestinal organisms. Agglutinating activity was unaffected by trypsin or acid but it was abolished rapidly by pepsin. Both colostral and gastrointestinal IgA agglutinated a wide range of enteric organisms. Variations in this activity occurred between different individua...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1966
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.20-2339