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Involvement of carbohydrate moieties in the heterogeneities of human blood clotting factor IX
Author(s) -
Polack Benoǐt,
Freyssinet JeanMarie
Publication year - 1986
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150070905
Subject(s) - wheat germ agglutinin , glycoprotein , immunoelectrophoresis , sodium dodecyl sulfate , chemistry , lectin , polyacrylamide gel electrophoresis , carbohydrate , clotting factor , electrophoresis , biochemistry , polyacrylamide , homogeneous , sodium , blood clotting , chromatography , biology , antigen , immunology , enzyme , polymer chemistry , medicine , physics , organic chemistry , thermodynamics
Abstract Purified human blood clotting factor IX, although homogeneous by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, showed two peaks when analyzed by crossed immunoelectrophoresis in the presence of calcium. Differential affinity of lectin from wheat germ (WGA) for the two forms of factor IX, detected by crossed affino‐immunoelectrophoresis, demonstrated that carbohydrate moieties are involved in factor IX heterogeneities. The slow migrating peak has a higher affinity for WGA ( K d = 5.26 × 10 −7 M) than the fast migrating peak ( K d = 1.29 × 10 −5 M). This study emphasizes the usefulness of lectins as tools to assess homogeneity and integrity of glycoproteins.