JBC, Vol. 251, Issue 15, 4673-4679, Aug, 1976
Characterization of mannose-labeled glycopeptides from human diploid cells and their growth-dependent alterations
T. Muramatsu, N. Koide, C. Ceccarini and P. H. Atkinson
Mannose-labeled glycopeptides were prepared from human diploid fibroblasts
harvested by brief pronase digestion. Combined use of
endo-beta-N-acetylglucosaminidase H and D converted most of the
mannose-label into arrays of oligosaccharides. They were separated by paper
chromatography and were characterized by Sephadex G-25 column
chromatography, by affinity column chromatography on concanavalin
A-Sepharose, and by successive digestion with alpha-mannosidase and
beta-mannosidase. The results indicated that mannose residues existed as
clusters of various sizes, which we refer to as "oligomannosyl cores". The
large oligomannosyl cores (approximately 7 to 8 mannosyl residues) were
predominant in the glycopeptides from growing cells and were preferentially
associated with neutral glycopeptides, similar to Unit A glycopeptides of
thyroglobulin (mannose-N-acetylglucosamine unit). In glycopeptides from
nongrowing cells, the ratio of the large oligomannosyl cores decreased,
accompanying the increase of a small oligommanosyl core consisting of 3
mannosyl residues. The small core was preferentially associated with acidic
glycopeptides.
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