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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1981-6-13
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pubmed:abstractText |
The structure of the N-terminal 21 residues of the blood group Mg-specific major human erythrocyte membrane sialoglycoprotein was investigated, using tryptic MgM peptides and secondary fragments prepared by staphylococcal V8 protease treatment. The sequence Leu-Ser-Thr-Asn-Glu was obtained for the N-terminal five residues. Therefore, the Mg gene appears to have evolved from a Thr leads to Asn mutation of an N allele. This alteration was found to prevent the glycosylation of the amino acids at the second and third positions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
|
pubmed:issn |
0018-4888
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
362
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
81-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7216164-Amino Acid Sequence,
pubmed-meshheading:7216164-Blood Group Antigens,
pubmed-meshheading:7216164-Erythrocyte Membrane,
pubmed-meshheading:7216164-Erythrocytes,
pubmed-meshheading:7216164-Humans,
pubmed-meshheading:7216164-Peptide Fragments,
pubmed-meshheading:7216164-Sialoglycoproteins
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pubmed:year |
1981
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pubmed:articleTitle |
Amino acid sequence of the blood group Mg-specific major human erythrocyte membrane sialoglycoprotein.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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