In:
European Journal of Biochemistry, Wiley, Vol. 170, No. 1-2 ( 1987-12), p. 69-75
Abstract:
Electrophoretic analysis of endoglycosidase‐treated tissue plasminogen activator obtained from human melanoma cells showed that the heterogeneity observed for the protein in these preparations is caused by an N ‐glycosidically linked N ‐acetyllactosamine type of carbohydrate chain which is present in about 50% of the molecules. An oligomannose type and an N ‐acetyllactosamine type of glycan is present in all molecules. Three glycopeptides were isolated and characterized by 1 H‐NMR, sugar determination, methylation analysis and amino acid determination. The exact attachment site for each of the three glycans could be deduced from the amino acid compositions of the glycopeptides. Asn‐117 carries the oligomannose type of glycan, the structure of which was completely determined. Asn‐184 is the site where the presence or absence of a biantennary N ‐acetyllactosamine type of glycan causes the size heterogeneity. The third N ‐glycosylation site, Asn‐448, was found to carry a triantennary or tetraantennary N ‐acetyllactosamine type of carbohydrate chain.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1987.170.issue-1-2
DOI:
10.1111/j.1432-1033.1987.tb13668.x
Language:
English
Publisher:
Wiley
Publication Date:
1987
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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