Linked Life Data

8183324

Source:http://linkedlifedata.com/resource/pubmed/id/8183324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-6-16
pubmed:abstractText
The pattern of tyrosine-phosphorylated proteins is developmentally regulated in Trypanosoma brucei. To examine the function and regulation of these tyrosine-phosphorylated molecules, monoclonal antibodies were generated using purified tyrosine-phosphorylated proteins as immunogens. Two monoclonal antibodies were obtained. Both react with a set of proteins at 44-46 kDa, collectively referred to as pp44/46, that are phosphorylated on serine and tyrosine. Differentiation of the parasite from slender bloodforms to procyclic forms was accompanied by increased abundance and tyrosine-phosphorylation of pp44/46. The monoclonal antibodies immunoprecipitated protein kinase activity capable of phosphorylating pp44/46 on serine and tyrosine, and myelin basic protein on serine. The data indicate that the prominent tyrosine-phosphorylated proteins induced upon differentiation are either themselves protein kinases or that they are associated with protein kinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-78
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Developmental regulation of pp44/46, tyrosine-phosphorylated proteins associated with tyrosine/serine kinase activity in Trypanosoma brucei.
pubmed:affiliation
Seattle Biomedical Research Institute, WA 98109.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't