A study of the influence of newly synthesized acyclonucleosides and 1,2,3,4-tetrahydroisoquinoline derivatives on deoxythymidine and deoxycytidine kinase activities in human neurofibrosarcoma and ovarian cancer.

The influence of nine newly synthesized uracil acyclonucleosides, and 36 derivatives of 1,2,3,4-tetrahydroisoquinoline on the activity of enzymes catalysing dTMP and dGMP synthesis, on the content of dTTP and dGTP in acid soluble fraction and on the incorporation of [14C]dThd and [14C ]dGuo into DNA in tumour homogenates was studied. The influence of the compounds was studied in the cytosol from intraoperatively excised human tumours - neurofibrosarcoma and ovarian cancer. It was shown that dTMP and dGMP synthesis is inhibited competitively by 34.

Pyrimidine and purine salvage deoxyribonucleoside metabolism in hepatic and renal homogenates from rats pretreated with propylthiouracil or L-thyroxine.

OBJECTIVES: In vitro activities of thymidine kinase (TK, EC 2.7.1.

Thymidine kinase and adenosine kinase activities in homogenates of thyroid lobes in hemithyroidectomized rats; effects of melatonin in vitro.

OBJECTIVES: Thymidine kinase (TK, EC 2.7.1.

Further studies on cytostatic activity of alkoxymethyl purine and pyrimidine acyclonucleosides.

The influence of 14 acyclonucleosides, derivatives of adenine, guanine, uracil and thymine on the phosphorylation of dAdo, dGuo, dCyd and dThd occurring in the cytosol of growing amelanotic melanoma transplanted to Syrian hamsters, as well as on inhibition of tumor growth were studied. From among the studied ACNs eight were tested earlier (Modrzejewska et al., 1996, The influence of alkoxymethyl purine and pyrimidine acyclonucleosides on growth inhibition of Kirkman-Robbins hepatoma and possible mechanism of their cytostatic activity, Z.

Thymidine kinase activity in homogenates of rat thyroid lobes from euthyroid, hypothyroid and/or hyperthyroid rats incubated with EGF: studies ex vivo in vitro.

Objective: To examine thymidine kinase (TK - ATP: thymidine 5'-phosphotransferase, EC 2.7.1.