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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1998-1-9
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pubmed:abstractText |
Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several alpha-lactalbumins of both ruminant and nonruminant species are known to be glycosylated. In all these species the glycosylation site is the 45Asn in the usual triplet 45Asn-Gly/Gln-47Ser. We have found that human alpha-lactalbumin is glycosylated and the glycosylation site has been determined by protein sequencing and mass spectrometry. We report an unusual glycosylation site at 71Asn in the triplet 71Asn-Ile-73Cys, which is conserved in all known alpha-lactalbumins except red-necked wallaby. That a relatively small proportion of the protein is glycosylated (about 1%) may reflect the importance of this region of the protein sequence to the molten globule state of alpha-lactalbumin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0277-8033
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
747-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9365923-Amino Acid Sequence,
pubmed-meshheading:9365923-Binding Sites,
pubmed-meshheading:9365923-Conserved Sequence,
pubmed-meshheading:9365923-Female,
pubmed-meshheading:9365923-Glycosylation,
pubmed-meshheading:9365923-Humans,
pubmed-meshheading:9365923-Lactalbumin,
pubmed-meshheading:9365923-Mass Spectrometry,
pubmed-meshheading:9365923-Molecular Sequence Data,
pubmed-meshheading:9365923-Oligopeptides,
pubmed-meshheading:9365923-Sequence Analysis
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pubmed:year |
1997
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pubmed:articleTitle |
The unusual amino acid triplet Asn-Ile-Cys is a glycosylation consensus site in human alpha-lactalbumin.
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pubmed:affiliation |
Centro Studio Alimentazione Animali, CNR, Torino, Italy.
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pubmed:publicationType |
Journal Article
|