N-acetyl-β- d-glucosaminyltransferases related to the synthesis of mucin-type glycoproteins in human ovarian tissue

• Published in: Carbohydrate research 1986-06, Vol.149 (1), p.241-252
• Main Authors: Yazawa, Shin, Abbas, Saeed A., Madiyalakan, Ragupathy, Barlow, Joseph J., Matta, Khushi L.
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Applied sciences; Biological and medical sciences; Carbohydrate Conformation; Carbohydrate Sequence; Carbon Radioisotopes; Enzymes and enzyme inhibitors; Exact sciences and technology; Female; Fundamental and applied biological sciences. Psychology; Glucosyltransferases - metabolism; Humans; Microsomes - enzymology; Mucins - biosynthesis; N-Acetylglucosaminyltransferases; Oligosaccharides - chemical synthesis; Other techniques and industries; Ovary - enzymology; Substrate Specificity; Transferases; Tritium
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/S0008-6215(00)90381-1

The presence of N-acetyl-β- d-glucosaminyltransferases in microsome preparations from human ovarian tissues was investigated with UDP-GlcNAc and several synthetic oligosaccharides as acceptors. The products were identified by paper chromatography and the linkage of the 2-acetamido-2-deoxy-β- d-glucopyranosyl group incorporated into oligosaccharides was determined by exoglycosidase digestions, 1H-n.m.r. spectroscopy, and methylation analysis. These results showed that ovarian microsome preparations contain both β-(1→3)- and β-(1→6)- N-acetyl- d-glucosaminyltransferase activities which might be involved in the synthesis of mucin-type glycoproteins. Substrate competition tests suggests that both UDP-GlcNAc:-Bn glycoside of β- d-Glc pNAc-(1→6)-α- d-Gal pNAc [GlcNAc to GalNAc] and -Bn glycoside of β- d-Gal p-(1→3)-[β- d-GlcNAc-(1→6)]-α- d-Gal pNAc [GlcNAc to Gal] β-(1→3)- N-acetyl- d-glucosaminyltransferase activities reside in a single enzyme species.