ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
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 (Kd= 5.26 × 10-7 M) than the fast migrating peak (Kd= 1.29 × 10-5 M). This study emphasizes the usefulness of lectins as tools to assess homogeneity and integrity of glycoproteins.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150070905
