Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Synthetic chocolate colourant, flavourant and the mixture of both were administered to healthy adult male albino rats to evaluate their effect on the nucleic acids metabolism, i.e. deoxyribonucleic and ribonucleic acids (DNA and RNA), total serum protein, thyroid hormones (T4 and T3) and nuclease enzymes, i.e. cytoplasmic- and mitochondrial deoxyribonuclease and ribonuclease (DNase and RNase) in brain, liver, and kidneys. Also, the activity of the fundamental enzymes of the oxidative pentose phosphate pathway, i.e. cytoplasmic and mitochondrial glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase (G-6-PD and 6-PGD), as well as total lipids and cholesterol contents in the same organs were studied. Ingestion of the studied food additives significantly increased serum protein, RNA and T4 hormone, while, DNA and T3 hormone were insignificantly elevated. In connection with this, the hydrolytic enzymes of nucleic acids (DNase and RNase activities) were stimulated by all studied food additives and in all mentioned organs. The activity of G-6-PD and 6-PGD in both cytoplasmic and mitochondrial fractions of all studied organs were increased. The highest increase was noticed in rats fed on diets supplemented with the mixture of both colourant and flavourant followed by colourant then flavourant, respectively.
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PMID:Biochemical effect of chocolate colouring and flavouring like substances on thyroid function and protein biosynthesis. 171 48

Pollack, J. D. (University of Connecticut, Storrs), Shmuel Razin, and Robert C. Cleverdon. Localization of enzymes in Mycoplasma. J. Bacteriol. 90:617-622. 1965.-Cells of eight parasitic and two saprophytic Mycoplasma strains were lysed by use of osmotic shock, and the membranes were separated from the soluble fraction by use of differential centrifugation. Cell fractions were tested for reduced nicotinamide adenine dinucleotide (NADH(2)) oxidase, reduced nicotinamide adenine dinucleotide phosphate (NADPH(2)) oxidase, glucose-6-phosphate dehydrogenase, adenosine triphosphatase, ribonuclease, and deoxyribonuclease activities. Adenosine triphosphatase was confined to the membrane fraction of all Mycoplasma strains. The NADH(2) oxidase activity was associated with the membranes of the saprophytic M. laidlawii and with the soluble fraction of the parasitic Mycoplasma strains. NADPH(2) oxidase activity was detected only in the soluble fraction of the parasitic strains. Glusose-6-phosphate dehydrogenase was demonstrated only in the soluble fraction of M. laidlawii. Ribonuclease activity was found usually in both membrane and soluble fractions, but was generally higher in the membrane fraction. In the human and bovine Mycoplasma strains, deoxyribonuclease activity could not be demonstrated in the soluble fraction; in the remaining strains, activity was highest in the soluble fraction. Dissolution of M. laidlawii strain B membranes by sodium deoxycholate significantly increased membrane-NADH(2) oxidase and adenosine triphosphatase activities.
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PMID:Localization of Enzymes in Mycoplasma. 1656 57