AI Article Synopsis
- The study examined the presence of antihistone antibodies in various commercial immunoglobulin preparations.
- The role of histones as cofactors in the binding of immunoglobulins and healthy sera to charged molecules like DNA and phosphatidylcholine was assessed.
- It was found that preincubating histones with certain molecules reduced their effectiveness as cofactors, while the interaction with natural antibodies suggested a reason for their ability to bind to multiple targets.
Article Abstract
The presence of antihistone antibodies was determined in different commercial immunoglobulin preparations. The ability of histones to perform the function of cofactor in interaction of immunoglobulin preparations and sera of healthy people with charged molecules such as DNA, cardiolipin and phosphatidylcholine, was determined. The addition of histones of immunoglobulin preparations or serum samples is accompanied by forming the stable complex, components of which interact with the charged molecules. The capacity of histones to play the role of cofactor is less evident in the case when they are preincubated with DNA or cardiolipin. The interaction of natural antibodies with histones can explain their polyspecificity in some cases.
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| http://dx.doi.org/10.1016/s0165-2478(96)02626-0 | DOI Listing |
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