Linked Life Data

9728401

Source:http://linkedlifedata.com/resource/pubmed/id/9728401

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-11-5
pubmed:abstractText
A low molecular weight mitogen (LMP) from Streptococcus pyogenes strain NY 5 was successively purified by adsorption on phenylsepharose, chromatography on Resource S and Superdex G 30 and finally by affinity chromatography on antiphosphothreonine agarose. The N-terminal protein sequence of the mitogen was determined. The occurrence of phosphoamino acids was investigated by immunoassay using monoclonal antibodies. The LMP is a threonine-phosphorylated protein different of HPR protein of PTS-system, its mitogenic activity was lost after treatment with streptococcal protein phosphatase or alkaline phosphatase. The inactivated LMP was activated by phosphorylation with phosphokinase and ATP. The active LMP was also inactivated in streptococcal cultures secreting acid protein phosphatase during the phase of phosphate limitation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0934-8840
pubmed:author
pubmed:issnType
Print
pubmed:volume
288
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-21
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Influence of the phosphorylation state on the biological activity of a low-molecular mitogen from group A streptococci.
pubmed:affiliation
Institut für Experimentelle Mikrobiologie, Friedrich-Schiller-Universität Jena (FSU), Germany.
pubmed:publicationType
Journal Article