PURIFICATION AND CHARACTERIZATION OF A NOVEL GLYCOPROTEIN WHICH HAS SIGNIFICANT HOMOLOGY TO HEAVY-CHAINS OF INTER-ALPHA-TRYPSIN INHIBITOR FAMILY FROM HUMAN PLASMA

Plasmapheresis with a dextran sulfate column is a treatment for patien ts with hypercholesteremia, When proteins bound to the column during t he treatment were fractionated to prepare some known proteins, we foun d a 57 kDa glycoprotein designated GP57 which showed a new N-terminal amino acid sequence, Western-blot analysis of human plasma revealed th at only a 120 kDa protein, GP120, reacted with anti-GP57 antibody, Sin ce GP120 and GP57 had an identical N-terminal amino acid sequence, GP1 20 is probably the intact form of GP57, The isoelectric point of GP120 was 6.8, N-Glycanase treatment decreased the molecular weight of GP12 0 by 15 kDa, Neuraminidase and O-glycanase, however, did not affect th e molecular weight, Amino acid sequence analyses of the lysylendopepti dase digest of GP120 revealed significant homology to the heavy chains of inter-alpha-trypsin inhibitor (ITI) family, Since GP120 showed no bikunin sequence, and chondroitinase treatment and alkaline treatment of GP120 did not affect its molecular weight, we concluded that GP120 was not a complex with bikunin, We designated GP120 as IHRP (ITI heavy chain-related protein).