DOI: 10.1073/pnas.74.1.134. Enzymatic conversion of proteins to glycoproteins.

Enzymatic conversion of proteins to glycoproteins.

10.1073/pnas.74.1.134

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The enzymatic transfer of the oligosaccharide moiety from an oligosaccharide-lipid to denatured forms of three secretory proteins--ovalbumin, alpha-lactalbumin, and ribonuclease A--has been demonstrated utilizing a membrane fraction from hen oviduct. Based on a survey of 10 proteins denatured by sulfitolysis, the presence of the tripeptide sequence -Asn-X-Thr-Ser- (X represents a variable amino acid) appears to be necessary but not sufficient for the protein to serve as acceptor in vitro. The results of this investigation also suggest that unfolding of the polypeptide chain is required in order to expose sites for carbohydrate attachment.

Bibliography

Pless, D. D., & Lennarz, W. J. (1977). Enzymatic conversion of proteins to glycoproteins. Proceedings of the National Academy of Sciences, 74(1), 134â138.

Authors 2

D D Pless (first)
W J Lennarz (additional)

References 0 Referenced 206

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 3:21 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 11:08 a.m.)
Indexed	1 week, 4 days ago (Aug. 23, 2025, 1:02 a.m.)
Issued	48 years, 8 months ago (Jan. 1, 1977)
Published	48 years, 8 months ago (Jan. 1, 1977)
Published Online	48 years, 8 months ago (Jan. 1, 1977)
Published Print	48 years, 8 months ago (Jan. 1, 1977)

Funders 0

None

BibTeX

@article{Pless_1977, title={Enzymatic conversion of proteins to glycoproteins.}, volume={74}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.74.1.134}, DOI={10.1073/pnas.74.1.134}, number={1}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Pless, D D and Lennarz, W J}, year={1977}, month=jan, pages={134–138} }

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