0100488898

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STUDIES ON MANNOSYL GLYCOPROTEINS OF CULTURED FIBROBLASTS

English (英語)

The Kobe journal of the medical sciences

24(1)

17-30

1978-03

[3H]mannose-labeled glycoproteins were prepared from cultured rat fibroblasts by solubilization with Triton X-100. They were separated into two fractions by affinity column chromatography on con A-Sepharose, namely weakly adsorbed fraction (those eluted by methyl α-mannoside) and strongly adsorbed fraction (those recovered only by sodium dodecyl sulfate). Glycopeptides were prepared from each fraction by pronase digestion and were analyzed by digestion with endo-β-N-acetylglucosaminidases. The result indicated that most of [3H]mannose-labeled glycoproteins were adsorbed to con A-Sepharose, and that separation into the two fractions depended at least partly on the size of oligomannosyl cores, i.e. mannosyl glycoproteins with larger cores were strongly adsorbed to the column and those with smaller cores were weakly adsorbed. Molecular species of the mannosyl glycoproteins adsorbed to the column of con A-Sepharose were analyzed by SDS disc gel electrophoresis. The electrophoretogram of the both fractions showed broad peaks, indicating the complexity of mannosyl glycoproteins. However, the major peak in each fraction was different to each other, i.e. molecular weight about 100,000 for strongly adsorbed fraction and molecular weight about 55,000 for weakly adsorbed fraction. Then, the iodinated cell surface proteins from rat fibroblasts were separated by con A-Sepharose column and analyzed by disc gel electrophoresis. Molecular species in the strongly adsorbed fraction and weakly adsorbed fraction were again found to be different.

mannosyl glycoproteins

紀要論文