期刊
BIOCHEMICAL JOURNAL
卷 355, 期 -, 页码 245-248出版社
PORTLAND PRESS LTD
DOI: 10.1042/0264-6021:3550245
关键词
N-linked oligosaccharide; oligosaccharyltransferase
Bovine DNase I contains two potential N-linked glycosylation sites with the sequences Asn(18)-Ala-Thr and Asn(106)-Asp-Ser. A previous report established that pancreatic DNase I has only one sugar chain at Asn(18) [Liao, Salnikow, Moore and Stein (1973) J. Biol. Chem. 248, 1489-1495]. We found, however. that bovine DNase I expressed in COS-1 cells was glycosylated about 70% at Asn(106) in addition to being completely glycosylated at Asn(18) Glycosylation of Asn(106) increased to 97%, when Asp(107) was mutated to Glu or when Ser(108) was mutated to Thr. Mutation of Asp(107) to Trp had no effect, whereas a substitution with Pro at this position abolished glycosylation of Asn(106). Analysis of the state of glycosylation of DNase I purified from a variety of bovine tissues revealed that DNase I from spleen, submaxillary gland, lung and adrenal had two sugar chains, whereas enzyme from pancreas and kidney had only one sugar chain. These findings demonstrate a major difference in the ability of various tissues to utilize N-linked glycosylation signals that contain suboptimal residues in the second and third positions.
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