Embryoglycan is the high-molecular-weight
poly-N-acetyllactosamine characteristically and abundantly present in early embryonic cells. Among
lectins reacting with poly-N-acetyllactosamines pokeweed
agglutinin (PWA) was found to be most useful in analyzing
glycoproteins from HM-1 pluripotent
embryonal carcinoma (EC) cells, since virtually all
glycoproteins carrying
embryoglycan in these cells could be isolated by affinity chromatography on PWA-
agarose. Furthermore almost all of
embryoglycan from HM-1 cells bound to PWA-
agarose. Since PWA-
agarose used for the present study was confirmed to bind branched but not linear poly-N-acetyllactosamines, the above result indicated that
embryoglycan lacking branched poly-N-acetyllactosaminyl chain was scarcely present in these cells. The same approach was used as a mean to show that
embryoglycan with
Lotus tetragonolobus agglutinin receptor activity also usually has the branched
poly-N-acetyllactosamine structure in EC cells.
Glycoprotein fractions from PYS-2 parietal endoderm cells and from STO fibroblasts also bound to PWA-
agarose. However, the ratio of PWA binding fraction to the total [14C]
galactose-labeled
glycoproteins was less in these cells as compared to the value in EC cells, and the poly-N-acetyllactosamines from these cells exhibited lower molecular weights than
embryoglycan. These results are consistent with our proposal that the complexity and abundance of poly-N-acetyllactosamines distinguishes EC cells from most other cells.