Linked Life Data

1378706

Source:http://linkedlifedata.com/resource/pubmed/id/1378706

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-8-14
pubmed:abstractText
The assay of acidic peptides as substrates for protein kinases has not been as easy to perform as testing basic peptides or polypeptides. We have developed a simple, rapid, and cost-effective procedure that allows the design and testing of potential peptide substrates without the constraints imposed by the phosphocellulose filter paper method (the need to incorporate positively charged residues into the peptide sequence). The technique combines the chelation of 32Pi by acid molybdate with PEI-cellulose chromatography. In this way the migration of 32P-labeled Pi, ATP, and protein are impeded while phosphopeptide is eluted in 1.5 ml from a 0.25-ml disposable column. In order to validate the assay we used two angiotensin II analogues as peptide substrates for the protein tyrosine kinase pp60c-src. The assay results using the new procedure were compared to those of the phosphocellulose filter paper technique. We also demonstrated the use of this method to test linear and cyclic peptides that could not be assayed with the phosphocellulose paper technique. This assay will aid those who are attempting to determine the substrate specificity of protein kinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-51
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1378706-Adenosine Triphosphate, pubmed-meshheading:1378706-Amino Acid Sequence, pubmed-meshheading:1378706-Animals, pubmed-meshheading:1378706-Autoradiography, pubmed-meshheading:1378706-Cell Line, pubmed-meshheading:1378706-Chromatography, High Pressure Liquid, pubmed-meshheading:1378706-Chromatography, Ion Exchange, pubmed-meshheading:1378706-Chromatography, Thin Layer, pubmed-meshheading:1378706-Insects, pubmed-meshheading:1378706-Molecular Sequence Data, pubmed-meshheading:1378706-Peptides, pubmed-meshheading:1378706-Phosphopeptides, pubmed-meshheading:1378706-Phosphorus Radioisotopes, pubmed-meshheading:1378706-Protein Kinases, pubmed-meshheading:1378706-Proto-Oncogene Proteins pp60(c-src), pubmed-meshheading:1378706-Substrate Specificity, pubmed-meshheading:1378706-Transfection
pubmed:year
1992
pubmed:articleTitle
An assay for acidic peptide substrates of protein kinases.
pubmed:affiliation
Department of Neuro-Oncology, University of Texas M. D. Anderson Cancer Center, Houston 77030.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't