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Characterization of human deoxycytidine kinase. Correlation with cDNA sequences
S Eriksson1, E Cederlund, T Bergman
1Medical Nobel Institute, Department of Biochemistry, Karolinska Institutet, Stockholm, Sweden.
FEBS Letters
|March 25, 1991
Summary
Human deoxycytidine kinase (dCK) structure data is conflicting. Peptide analysis reveals dCK is a 30.5 kDa protein, not the previously reported 71 kDa form, with similarities to other kinases.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Conflicting data exists regarding the molecular weight and structure of human deoxycytidine kinase (dCK).
- Previous reports suggested a monomeric 60 kDa form and a cDNA encoding a 71 kDa protein.
- Pure dCK isolated from leukemic spleen presented as a dimer of 30 kDa subunits.
Purpose of the Study:
- To resolve discrepancies in the reported structure of human deoxycytidine kinase (dCK).
- To characterize the peptide structure of purified dCK from leukemic spleen.
- To compare peptide sequences with existing cDNA data and related kinases.
Main Methods:
- Peptide sequencing of purified deoxycytidine kinase (dCK) from leukemic spleen.
- Comparison of obtained peptide sequences with cloned cDNA sequences.
- Homology analysis of dCK peptide sequences against known kinase families.
Main Results:
- Peptide sequences from purified dCK did not match the cDNA for the 71 kDa protein.
- Peptide sequences corresponded to a recently cloned cDNA for a 30.5 kDa dCK.
- Detected homology between dCK peptide sequences and parts of thymidine kinases and protein-tyrosine kinases.
Conclusions:
- Human deoxycytidine kinase (dCK) is likely a 30.5 kDa protein, existing as a dimer.
- The previously reported 71 kDa dCK structure may be inaccurate or represent a different entity.
- dCK shares structural homologies with thymidine kinases and protein-tyrosine kinases, suggesting functional relationships.