title: Enzymatic conversion of proteins to glycoproteins.
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.
mesh_terms: D000818:Animals; D002645:Chickens; D005260:Female; D006017:Glycolipids / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D007768:Lactalbumin / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism*; D010047:Ovalbumin / Q000378:metabolism; D010057:Oviducts / Q000201:enzymology*; D011489:Protein Denaturation; D012260:Ribonucleases / Q000378:metabolism; D013329:Structure-Activity Relationship; D013447:Sulfites
chemical_list: D006017:Glycolipids; D006023:Glycoproteins; D008563:Membrane Lipids; D009844:Oligosaccharides; D013447:Sulfites; D010047:Ovalbumin; D007768:Lactalbumin; D012260:Ribonucleases
references.citation: J Biol Chem. 1974 Feb 10;249(3):818-24
references.pmid: 4204553
references.citation: Biochemistry. 1971 Jun 22;10(13):2606-17
references.pmid: 4326772
references.citation: J Biol Chem. 1975 Nov 10;250(21):8569-75
references.pmid: 389
references.citation: Proc Natl Acad Sci U S A. 1974 Jun;71(6):2391-5
references.pmid: 4526213
references.citation: J Biol Chem. 1973 Jan 25;248(2):707-10
references.pmid: 4734333
references.citation: J Biol Chem. 1973 Feb 25;248(4):1489-95
references.pmid: 4734471
references.citation: J Biol Chem. 1973 Nov 10;248(21):7570-9
references.pmid: 4745783
references.citation: J Biol Chem. 1972 Apr 25;247(8):2629-31
references.pmid: 5019965
references.citation: Annu Rev Biochem. 1976;45:95-112
references.pmid: 786163
references.citation: Eur J Biochem. 1976 Apr 1;63(2):441-8
references.pmid: 1261555
references.citation: J Biol Chem. 1975 Sep 10;250(17):7014-9
references.pmid: 1158894
references.citation: J Biol Chem. 1975 Sep 10;250(17):7006-13
references.pmid: 1158893
references.citation: Biochem J. 1975 Feb;146(2):299-307
references.pmid: 1156375
references.citation: J Biol Chem. 1975 Mar 25;250(6):1992-2002
references.pmid: 1167860
references.citation: Biochem Biophys Res Commun. 1970 May 22;39(4):757-65
references.pmid: 5490222
references.citation: Biochemistry. 1965 Aug;4(8):1473-8
references.pmid: 5863314
references.citation: J Biol Chem. 1964 Aug;239:2530-8
references.pmid: 14235531
references.citation: Nature. 1960 Nov 26;188:721-4
references.pmid: 13723142
references.citation: J Biol Chem. 1958 Dec;233(6):1364-72
references.pmid: 13610844
references.citation: J Biol Chem. 1957 Oct;228(2):835-45
references.pmid: 13475364
references.citation: J Biol Chem. 1951 Nov;193(1):265-75
references.pmid: 14907713
references.citation: Biochem Soc Symp. 1974;(40):17-26
references.pmid: 4620382
references.citation: Carbohydr Res. 1976 Jul;49:455-73
references.pmid: 986874
references.citation: J Biol Chem. 1976 Sep 25;251(18):5490-5
references.pmid: 965372
references.citation: Proc Natl Acad Sci U S A. 1970 Jul;66(3):975-82
references.pmid: 4193390
references.citation: J Bacteriol. 1973 Feb;113(2):874-83
references.pmid: 4632325