Search results for "Choline kinase"

Isolierung und charakterisierung einer cholinkinase aus Phaseolus vulgaris L.-Keimlingen

1977

Summary The enzyme choline kinase (ATP: Choline phosphotransferase E.C. 2.7.1.32) was extracted and partially purified from hypocotyl hooks of Phaseolus vulgaris L. seedlings. K m -value and pH-dependence of the activity were determined. The amount of enzyme activity in extracts depended on light conditions used for plant growth. Etiolated seedlings showed much lower enzyme levels than those grown in white light. Blue and red light conditions decreased enzyme levels below dark values. The in vitro enzyme activity was influenced by inhibitors and growth regulators. The enzyme activity was stimulated by Atropine, 2-Chloroethylammoniumchloride (Cycocel) and Gibberellic acid and was inhibited b…

New more polar symmetrical choline kinase inhibitors II: Study of setting up a new scaffold for the cancer therapy

2015

Thymidine-, uridine- and choline-kinase in rabbit kidney cells infected with herpesvirus hominis, type I and II.

1972

Data are presented about the activity of the thymidine-, uridine- and choline-kinase after infection with 21 strains ofherpesvirus hominis of serotype I or II in rabbit kidney cells. Type I strains increase the activity of the thymidine-kinase 15–20 fold over the controls, whereas the type II strains demonstrate a moderate activity, the level of the enzyme is increased 2–5 fold. One giant cell forming strain exhibits unusual properties, the TK activity decreases in correlation to the controls. The uridine- and choline-kinases induce the respective enzymes in different manner. The strains tested are divided into 5 groups depending upon the activity of the enzymatic activity. The implications…

Inhibition of giant cell formation by compound 48/80 after infection with herpesvirus hominis

1974

Choline kinase has been found to be a soluble enzyme with a molecular weight of 105,000 in the cytoplasm of primary rabbit kidney cells. It has been purified 150-fold. It was investigated whether the inhibiting effect of Cpd 48/80 on virus-induced giant cell formation is due to interference with this enzyme. Cpd 48/80-dimer was shown to inhibit the choline kinase activityin vitro without a concomitant inhibition of giant cell formation. Likewise, another competitive inhibitor of choline kinase, purinyl-6-histamine, does not prevent giant cell formation. This finding suggests that there is no correlation between choline kinase activity and giant cell formation.