Delayed luminescence of high homeopathic potencies on sugar globuli.

Delayed luminescence signals of Arg.met. CMf (100Mf), Canth. CMf, Bov. CMf absorbed onto sugar globuli was observed by exciting them at their known resonance frequency of 2.060 MHz. Arn. CMf also showed delayed luminescence when excited at 2.060 MHz and at 1.828 MHz. Alc. LMK (50MK) could not be excited by 2.060 MHz and showed properties of control globuli. Canth. LMK could not be excited at 2.006 MHz. The delayed luminescence signals were characterized by the coefficient B(2) typical of the delayed luminescence of non-living complex systems, and by the coefficient B(0) typical of living systems. Both coefficients can be considered as indicative of holistic quantum structures in homeopathic potencies.

Allosteric effects of cortisol, estradiol, progesterone and of the DNA-sequences poly d(A-T) and poly d(C-G) on the adenosine and thymidine phosphorylating activity of the nuclear nucleoside-nucleotide phosphotransferase C.

The ATP-synthesis of the nuclear nucleoside-nucleotide phosphotransferase C was stimulated by progesterone alone and in combination with poly d(A-T) at 10(-10)-10(-9) M, by estradiol/poly d(A-T) at 5-10(-9) M, by cortisol alone and in combination with poly d(A-T) at 10(-9)-10(-8) M and by poly d(A-T) alone. No effect was observed using poly d(C-G). Using increasing adenosine/dTTP as substrates, cortisol, progesterone, estradiol/poly d(A-T) and poly d(A-T) alone caused positive cooperativity of the substrate saturation curves of the allosteric enzyme C by lowering the apparent Ks 0.5-values and by altering Vmax. The dTTP-synthesis of enzyme C was stimulated by both poly d(A-T) and poly d(C-G) alone and in combination with low estradiol (up to 10(-10) M)-and with higher progesterone concentrations (10(-8)-10(-7) M), whereas cortisol inhibited at higher concentrations completely. Using increasing thymidine/ATP as substrates progesterone and estradiol, also in combination with poly d(A-T) were positive effectors of the substrate saturation curves of enzyme C. By this, the apparent Ks 0.5-values or Vmax were changed. Cortisol could be shown to be a negative effector.

Nucleoside triphosphate syntheses by chromatin bound enzymes from Morris hepatoma 9121 nuclei.

1. Enzymatic syntheses of deoxyribo- and ribonucleoside triphosphates were observed with purified, chromatin bound enzyme C from Morris Hepatoma 9121 nuclei. 2. Intermediate substrates were nucleoside mono- and diphosphates for enzyme C. 3. The three phosphate residues of ATP serving as energy-rich phosphate donor were successively transferred to a nucleoside substrate by enzyme C.

Characterization of six nucleoside-nucleotide phosphotransferases from the chromatin of Morris hepatoma 9121 cells by physicochemical and biochemical techniques.

1. Six nucleoside-nucleotide phosphotransferases A-F were isolated from chromatin of Morris Hepatoma 9121 cells and characterized. 2. The apparent mol wt are: 13,000 daltons for A, 35,000 or 70,000 for B and E, 240,000 for C, 180,000 for D and 300,000-400,000 for F. 3. The sedimentation values are: 2.5-3 S for A, 3 or 5 S for B and E, 11 S for C, 7-8 S for D and 14 S for F. 4. The activity of the six enzymes A-F was stimulated with 1-2.5 micrograms calf thymus DNA using thymidine/ATP as substrates. 5. In the presence of defined polydeoxynucleotides, each enzyme A-F showed a differential preference for its substrates.