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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1977-9-22
|
| pubmed:abstractText |
A seed protein with an apparent molecular weight of 5000 has been isolated and purified from Ricinus communis. This protein has a very high content of glutamine and an unusual ultraviolet absorption spectrum. The amino-terminal sequence of 22 residues determined by automatic Edman degradation is: NH2-Pro-Ser-Gln-Gln-Gly-Cys-Cys-Gly-Gln-Ile-Gln-Glu-Gln-Gln-Asn-Leu-Arg-Gln-Cys-Gln-Glu-Tyr-.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
492
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
364-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1977
|
| pubmed:articleTitle |
Isolation and characterization of a low-molecular weight seed protein from Ricinus communis.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|