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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1989-2-21
|
| pubmed:abstractText |
Bovine S-antigen purified in the presence of proteinase inhibitors contained a protein (30%) having an acetylated N-terminus (Ac-Met-Lys-Ala-Asn-Lys-Pro-Ala...) and a protein (70%) having an N-terminus unblocked but four residues less (Lys-Pro-Ala-Pro-Asn-His-Val-Ile-Phe...). Sequencing studies showed that uveitogenic peptides produced by chymotryptic digestion of S-antigen derived from the C-terminal half of the protein.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
994
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
191-3
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1989
|
| pubmed:articleTitle |
The amino acid sequence of S-antigen: N-terminus and uveitogenic peptides.
|
| pubmed:affiliation |
Institute for Protein Research, Osaka University, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|