O. Hosomi et al., SIMPLE PURIFICATION METHOD OF THE ANTIPHOSPHOLIPID ANTIBODY FROM NORMAL HUMAN PLASMA, Experimental and clinical immunogenetics, 14(4), 1997, pp. 281-285
We have reported that rabbit serum contains a phospholipid (PL)/gangli
oside-binding protein which adsorbs to Sephacryl S-400 gel and aggluti
nates human red blood cells. A new protein similar to the PL/gangliosi
de-binding protein was simply purified from normal human plasma using
Sephacryl S-400, Sepharose CL-4B and DEAE-Sepharose CL-6B columns. The
purified protein was found to agglutinate rabbit red blood cells. The
hemagglutination was specifically inhibited by two FL, phosphatidylse
rine and phosphatidylinositol, but not by any other FL, gangliosides,
saccharides or glycoproteins tested. From analyses of the N-terminal a
mino acid sequence and immunological specificity, the protein was iden
tified to be a human immunoglobulin M.