Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4-5
pubmed:dateCreated
1994-3-16
pubmed:abstractText
Deoxycytidine (CdR) kinase (E.C. 2.7.1.74) acts as a salvage enzyme in DNA biosynthesis, but little is known about this important nucleoside kinase in the brain. We report that CdR kinase activity in the 100,000 x g cytosolic fraction of normal adult rat brain cortex was 0.89 +/- 0.04 nmol/hr/mg protein which is twice that of the liver enzyme. For brain CdR kinase the apparent Km for CdR, ATP and Mg++ were 0.22, 1.1 and 0.63 mM, respectively. When the cytosolic preparation was incubated at 37 degrees C, CdR kinase activity rapidly decreased (t1/2 = 15 min); CdR (400 microM) protected the enzyme. Addition of DFDC (0 to 100 microM) competitively inhibited brain CdR kinase activity with Ki = 17 microM. DFDC elevated the apparent Km for CdR of brain CdR kinase 3.5-fold, from 0.22 to 0.8 mM. DFDC did not inhibit brain TdR kinase. AZT, which competitively inhibited TdR kinase (Ki = 0.6 microM), did not affect brain CdR kinase activity. These results indicate that the cytosol of rat brain contains CdR kinase which is inhibited by the deoxycytidine analog, DFDC. The enzyme is protected from thermal denaturation by CdR but not by TdR.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0965-0407
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Deoxycytidine kinase and thymidine kinase activities in rat brain.
pubmed:affiliation
Laboratory for Experimental Oncology, Indiana University School of Medicine, Indianapolis 46202-5200.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.