Linked Life Data

6392292

Source:http://linkedlifedata.com/resource/pubmed/id/6392292

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1985-1-25
pubmed:abstractText
The two basic Escherichia coli proteins that inhibit ornithine and arginine decarboxylase and were named provisionally antizyme 1 and antizyme 2 (Heller, J.S., Rostomily, R., Kyriakidis, D.A., and Canellakis, E.S. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 5181-5184) are shown to have long identical sequences with the ribosomal proteins S20/L26 and L34, respectively. We have also isolated ribosomal proteins from purified E. coli ribosomes by established methodology and further purified them by our purification procedure for antizymes 1 and 2. Of the various basic ribosomal proteins, two were found to have the same properties as antizyme 1 and 2. These results indicate that these two basic E. coli antizymes are ribosomal proteins. The nature of the acidic antizyme remains to be elucidated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15025-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Comparison of the basic Escherichia coli antizyme 1 and antizyme 2 with the ribosomal proteins S20/L26 and L34.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.