H
Hans Klenow
Researcher at University of Copenhagen
Publications - 49
Citations - 1522
Hans Klenow is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Deoxyadenosine & Adenosine. The author has an hindex of 22, co-authored 49 publications receiving 1514 citations.
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Journal ArticleDOI
Some properties of partially purified mammalian adenosine kinase.
TL;DR: Adenosine kinase has been partially purified from homogenates of rabbit liver and Ehrlich ascites tumor cells, and the kinase preparation obtained was free of adenosine deaminase and almost free ofadenosine triphosphatase activity.
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The N-terminal amino-acid sequences of DNA polymerase I from Escherichia coli and of the large and the small fragments obtained by a limited proteolysis.
TL;DR: The two fragments obtained by proteolytic cleavage of DNA polymerase I from Escherichia coli have been isolated by chromatography on hydroxyapatite and shows unambiguously that the small fragment is placed in the N-terminal end of the native enzyme.
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Proteolytic cleavage fo native DNA polymerase into two different catalytic fragments. Influence of assay condtions on the change of exonuclease activity and polymerase activity accompanying cleavage.
TL;DR: Treatment of native DNA polymerase from Escherichia coli with subtilisin may lead to its cleavage into a polymerase fragment and an exonuclease fragment which appears to depend on the conditions of the polymerase assay.
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Further studies on the effect of deoxyadenosine on the accumulation of deoxyadenosine triphosphate and inhibition of deoxyribonucleic acid synthesis in Ehrlich ascites tumor cells in vitro.
TL;DR: The inhibiting effect of deoxyadenosine on DNA synthesis is not completely reversed by deoxycytidine or deoxyguanosine separately but only by the two together, which is in relation to possible mechanisms of regulation of DNA synthesis.
Journal ArticleDOI
Proteolytic cleavage of DNA polymerase from Escherichia Coli B into an exonuclease unit and a polymerase unit
Hans Klenow,K. Overgaard-Hansen +1 more
TL;DR: The treatment of native DNA polymerase with subtilisin is reported on under conditions which lead to the cleavage of the enzyme into two separate subunits, one which is associated with exonuclease activity and the other with polymerase activity.