A monoclonal antibody that recognizes a cluster of a disaccharide, NeuAc alpha(2—-6)GalNAc, in mucin-type glycoproteins.

作者：Akira Kurosaka, Hiroshi Kitagawa, Shin Fukui, Y Numata, Hiroshi Nakada, Ikuo Funakoshi, Toshisuke Kawasaki, Toshio Ogawa, Hiroyuki Iijima, Ikuo Yamashina · 发表于：Journal of Biological Chemistry · 年份：1988 · DOI：10.1016/s0021-9258(18)68365-6 · 被引用次数：97 · 研究领域：Glycosylation and Glycoproteins Research、Carbohydrate Chemistry and Synthesis、Galectins and Cancer Biology

The structure of an epitopic carbohydrate recognized by a monoclonal antibody, MLS 102, was determined. A disaccharide, NeuAc alpha (2----6)GalNAc, the major prosthetic group of ovine submaxillary mucin (OSM) and related synthetic glycosides, NeuAc alpha(2----6)GalNAc alpha----Ser, NeuAc alpha(2----6)GalNAc beta----Ser, and NeuAc alpha (2----6)GalNAc beta----propyl, reacted with MLS 102 to similar extents, but the reaction was considerably weaker compared to that of OSM. This difference in reactivity could be ascribed to the occurrence of a cluster of the disaccharide on OSM. Purification of MLS 102-reactive antigens from a Triton X-100 extract of LS 180 cells by means of immunoaffinity chromatography gave mucin fractions (cMLS 102 antigen) with an OSM-like domain. Correlation between the content of the disaccharide, NeuAc alpha(2----6)GalNAc, in mucins and their reactivity with MLS 102 was observed.