Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1984-9-17
pubmed:abstractText
Murine B and T lymphocytes each contain a protein kinase activity that catalyzes the phosphorylation of both endogenous and exogenous substrates on tyrosine residues. In B lymphocytes, endogenous substrates of 56,000 and 60,000 daltons are found in the particulate fraction. Peptide mapping experiments indicate that these two substrates are closely related but are distinct from the major 58,000-dalton tyrosine protein kinase substrate found in T lymphocytes. To determine if the same kinase is active in both B and T lymphocytes, their substrate specificities were compared using two exogenously added substrates: angiotensin I and the cytoplasmic domain of the erythrocyte band 3 protein. LSTRA, a lymphoma cell line that expresses elevated levels of the T lymphocyte kinase (Casnellie, J. E., Harrison, M. L., Hellstrom, K. E., and Krebs, E. G. (1983) J. Biol. Chem. 258, 10738-10742), was used as a source of this enzyme. Kinetic analyses indicate that angiotensin I serves as a better substrate for the LSTRA kinase than for the B cell enzyme. Band 3, however, is preferentially phosphorylated by the B cell kinase. These results indicate that B and T lymphocytes express distinct tyrosine protein kinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9348-50
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
T and B lymphocytes express distinct tyrosine protein kinases.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't