Chemistry and Biochemistry of Glycoprotein sulfortansferases and Sulfate Acceptors

Abstract

Intestinal glycoprotein was purified from homogenized scraping of rat epithelial cell using gel chromatography. High molecular weight mucin was separated from low molecular weight protein by the help of chromatography. The purified glycoprotein were examined for purity by polyacrylamide gel electrophoresis. The carbohydrate and mino acid analysis of the purified glycoprotein shows the difference in sugars and mino acids. It appears that glycoprotein obtained from small intestine differs structurally. This reflection the presence of different type of glycosyle linkages in these glycoprotein. This study indicates that intestinal glycoprotein consists of at least three closely related high molecular weight glycoprotein which can be separated from other contaminants by the help of chromatographty.