Galactosyltransferases: Physical, Chemical, and Biological Aspect

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Abstract
Galactosyltransferases (GTs) are one of the members of a family of enzymes called glycosyltransferases involved in the biosynthesis of complex carbohydrates. These enzymes catalyze the transfer of galactose from UDP-galactose to an acceptor (glycoprotein, glycolipid) containing terminal N-acetylglucosamine or N-acetylgalactosamine residue. GTs occur in soluble (milk, serum, effusions, etc.) and insoluble (membrane) forms. The GT activities on the outer surface of the cells have been correlated with a host of cellular interactions, including fertilization, cell migration, embryonic induction, chondrogenesis, contact inhibition of growth, cell adhesion, hemostasis, intestinal cell differentiation, and immune recognition. GTs have been purified to homogeneity using affinity chromatography. Most GTs are found active in the pH range 6 to 8 and at temperatures between 35 to 40 degrees C. Manganese is an essential co-factor for GT activity. Isoenzymes of GT have been recognized, especially in tumor tissues, malignant effusions, and sera of cancer patients using polyacrylamide gel electrophoresis in the presence and absence of SDS. Depending on the source of the enzyme, the molecular weights of GTs range between 40,000 to 80,000 daltons. Carcinoma-associated GT isoenzyme has been reported to have a higher molecular weight than the normal GT isoenzyme. Development of monoclonal antibody against the cancer-specific GT isoenzyme will provide help in the development of an immunoassay for the measurement of this isoenzyme in the sera and an aid in the radioimmunolocalization of the tumors in cancer patients.

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