Linked Life Data

6452899

Source:http://linkedlifedata.com/resource/pubmed/id/6452899

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1981-7-23
pubmed:abstractText
An improved purification procedure is described for the rho transcription termination factor of Escherichia coli. The method involves lysozyme--sodium deoxycholate lysis, Polymin P fractionation, and chromatography on phosphocellulose, poly(uridylic acid)--Sepharose, and AMP--agarose. The method yields up to 9 mg of electrophoretically pure protein from 200 200 g of E. coli MRE 600. From quantitative amino acid analysis rho is calculated to have an E280nm (1%) of 3.7 +/- 0.3. The purified rho has an ATPase specific activity of 32 nmol of Pi released min-1 microgram-1 when poly(cytidylic acid) is used as a cofactor, and it functions effectively in termination of T7 DNA transcription. A subunit molecular weight of 48 000 for rho was determined by phosphate-buffered sodium dodecyl sulfate--polyacrylamide gel electrophoresis. The amino acid composition and circular dichroism spectrum in the far-ultraviolet for rho are presented.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1640-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Procedure for purification of Escherichia coli ribonucleic acid synthesis termination protein rho.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.