Binding of cytokines to pharmaceutically prepared human immunoglobulin.
نویسندگان
چکیده
منابع مشابه
High avidity IFN-neutralizing antibodies in pharmaceutically prepared human IgG.
This paper demonstrates and characterizes naturally occurring antibodies to interferon (IFN) in human IgG preparations. In vitro neutralization of the antiviral effect of IFN alpha and IFN beta, but not IFN gamma, was observed in 12 of 15 normal IgG preparations. The neutralizing capacity was higher against rIFN alpha 2A and rIFN alpha 2C than against lymphoblastoid IFN alpha and IFN beta. Früh...
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Background: Immunoglobulins (Igs) are protective glycoproteins specifically identify and eradicate microbes. Fragment of antigen binding (Fab) is a portion of antibody which binds to antigen and consists of one variable and one constant domain of one heavy and one light chain. Idiotypes, epitopes situated on Igs variable region, could be exploited to monitor and target malignant B cells and are...
متن کاملManganese and Iron Binding to Human Transferrin
The characteristics of manganese and iron binding to human apotransferrin (apo-tf) have been investigated and compared in this study. Both metal ions were taken up by human apo-tf and formed complexes, with the maximum absorbances observed at 410 and 340 nm for manganese-transferrin (Mn-tf) and 465 nm for iron-transferrin (Fe-tf). Addition of manganese (1.5 µg/ml) to the reaction mixture contai...
متن کاملManganese and Iron Binding to Human Transferrin
The characteristics of manganese and iron binding to human apotransferrin (apo-tf) have been investigated and compared in this study. Both metal ions were taken up by human apo-tf and formed complexes, with the maximum absorbances observed at 410 and 340 nm for manganese-transferrin (Mn-tf) and 465 nm for iron-transferrin (Fe-tf). Addition of manganese (1.5 µg/ml) to the reaction mixture contai...
متن کاملThe binding of human milk lactoferrin to immunoglobulin A.
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-Sepharo...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1993
ISSN: 0021-9738
DOI: 10.1172/jci116862