Forsch Komplementarmed
February 1999
Introduction: The oxidative degradation of urate to allantoin and CO2 is catalyzed by the enzyme uricase. Its activity was determined in the presence of two potassium cyanatum preparations in the dilution step D8, which differed by the method of preparation. While variant 1 (homoeopathic D8) was prepared homoeopathically, variant 2 (electronic D8) was produced electronically.
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March 1999
The physiological effects of the second messenger cAMP are displayed by cAMP-dependent protein kinase-medicated phosphorylation of specific target proteins which in turn control diverse cellular functions. We have determined this enzyme substrate phosphorylation in the presence of various glycosaminoglycans using a cAMP-dependent protein kinase isolated from rat liver. The results indicate that sulfated and unsulfated polysaccharides are able to inhibit phosphorylation of histone type IIa catalysed by cAMP-dependent protein kinase.
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January 1998
Characteristics and Efficiency of Homoeopathics from a Scientific Point of View 1. This work aims at the presentation of the specific peculiarities of homoeopathics as physics see it and at the explanation of their display of action by application of biochemical methods. 2.
View Article and Find Full Text PDFGlycosaminoglycans are long non-branched polysaccharides composed of repeating disaccharide units. In a previous in vitro study we have shown that such molecules are able to modulate substrate phosphorylation catalyzed by cAMP-dependent protein kinase. Here, we investigate the impact of glycosaminoglycans, such as heparan sulfate, dermatan sulfate, chondroitin 4- and 6-sulfate, keratan sulfate and hyaluronic acid upon adenylate cyclase, which directly regulates cAMP-dependent protein kinase activity via cAMP synthesis.
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