%0 Journal Article
%T PURIFICATION AND ANALYSIS OF CARBOHYDRATE CLUSTER FROM ERYTHROPOIETIN RECOMBINANT EXPRESSION RESULT ON THE LEAVEN SYSTEM OF Pichia pastoris
%A Andri Wardiana
%A Adi Santoso
%J Makara Seri Sains
%D 2011
%I Universitas Indonesia
%X For clinical purposes, pure protein and identification of carbohydrate structure from erythropoietin recombinant are needed. Purification was done with His-Trap affinity chromatography method and continued with gel filtration chromatography column to get purer protein. The carbohydrate cluster from the resulting pure protein then can be recognized by using N- and O-glycosidase and can be compared to EPO recombinant from mammal cells. The result showed similarity on the declining trend of the protein molecule¡¯s weight, which could be seen using the Western blot method. Pure oligosaccharide was hydrolyzed to produce various monosaccharide through incubation with HCl 4 N in 100 oC temperature for 6 hours and the result was applied on high intensity liquid chromatography incubator to learn the composition of its monosaccharide.
%K EPO
%K gel filtration chromatography
%K His-Trap affinity chromatography
%K monosaccharide
%U http://journal.ui.ac.id/science/article/viewFile/888/847