Linked Life Data

3130375

Source:http://linkedlifedata.com/resource/pubmed/id/3130375

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1988-6-20
pubmed:abstractText
There are 14 potential Asn-X-Thr/Ser glycosylation sites, or sequons, in the yeast external invertase sequence. Of these, 13 are wholly or partially glycosylated to give an average of 9-10 oligosaccharides/subunit (Reddy, V. A., Johnson, R. S., Biemann, K., Williams, R. S., Ziegler, F. D., Trimble, R. B., and Maley, F. (1988) J. Biol. Chem. 263, 6978-6985). On digestion of native holoenzyme by endo-beta-N-acetylglucosaminidase H (Endo H) an average of about seven oligosaccharides per subunit are released without affecting enzyme activity (Trimble, R. B., and Maley, F. (1977) J. Biol. Chem. 252, 4409-4412). To determine whether the remaining Endo H-resistant chains were restricted to a limited number of unique sequons or were randomly distributed on all 13, Endo H-treated native invertase was digested with either thermolysin or trypsin and the resultant glycopeptides isolated by reversed-phase high pressure liquid chromatography and gel filtration. It was found that the oligosaccharides attached to Asn92, Asn247, and Asn350 were partially resistant to Endo H, while those at Asn45 and Asn337) were completely resistant. Bio-Gel P-4 analysis revealed the Endo H-resistant oligosaccharides at Asn45, Asn92, Asn247, and Asn337 to be Man8-14GlcNAc, while the minor residual carbohydrate at Asn350 was Man greater than 50GlcNAc. The Endo H-susceptible oligosaccharides at Asn4, Asn146, and Asn256 were Man greater than 50GlcNAc while all other glycosylation sites contained Man8-14GlcNAc. Based on a hydropathic analysis of invertase, the two most Endo H-resistant oligosaccharides at Asn45 and Asn337 were located in the more hydrophobic regions of the molecule. These may form part of the folded protein structure or interacting subunit surfaces, thus restricting their accessibility to Endo H.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6986-92
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons.
pubmed:affiliation
Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.