Results 71 to 80 of about 686 (83)
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Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
Abstract The effectiveness of nicotinamide and 5′-methyl nicotinamide as inhibitors of nuclear NAD nucleosidase and poly ADP-ribose polymerase from rat liver has been investigated. Nicotinamide inhibited the NAD nucleosidase and the poly ADP-ribose polymerase with Ki's of 5 · 10−4 M and 2 · 10−5 M, respectively, 5′-methyl nicotinamide with Ki's of 3 ...
John B. Clark, G.M. Ferris, S. Pinder
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Abstract The effectiveness of nicotinamide and 5′-methyl nicotinamide as inhibitors of nuclear NAD nucleosidase and poly ADP-ribose polymerase from rat liver has been investigated. Nicotinamide inhibited the NAD nucleosidase and the poly ADP-ribose polymerase with Ki's of 5 · 10−4 M and 2 · 10−5 M, respectively, 5′-methyl nicotinamide with Ki's of 3 ...
John B. Clark, G.M. Ferris, S. Pinder
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Toxicon, 1975
Abstract Nicotinamide adenine dinucleotide nucleosidase (NAD glycohydrolase, EC 3.2.2.5) was demonstrated in venoms of various snakes. Among the venoms from 37 species of Viperidae, Crotalidae and Elapidae, venom of snakes in the genera Bungarus and Agkistrodon showed the highest activities.
Tomoji Suzuki +3 more
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Abstract Nicotinamide adenine dinucleotide nucleosidase (NAD glycohydrolase, EC 3.2.2.5) was demonstrated in venoms of various snakes. Among the venoms from 37 species of Viperidae, Crotalidae and Elapidae, venom of snakes in the genera Bungarus and Agkistrodon showed the highest activities.
Tomoji Suzuki +3 more
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Structural and biochemical basis of NAD+ nucleosidase activity of TIR domain-containing proteins
2021NAD+ (nicotinamide adenine dinucleotide) was first identified as a cofactor in many redox reactions. Subsequently, it has been found to synchronize many cellular functions through the regulation of NAD+ consuming enzymes like CD38, sirtuins, and PARPs (poly ADP-ribose polymerases).
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Folia Microbiologica, 1980
Purification of streptococcal extracellular NAD+ nucleosidase is associated with changes of kinetic properties. A high-molecular weight component is required for a full activity of the enzyme. The component is not produced by bacteria and is present in the Todd-Hewitt cultivation medium, the beef-heart extract serving primarily as its source.
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Purification of streptococcal extracellular NAD+ nucleosidase is associated with changes of kinetic properties. A high-molecular weight component is required for a full activity of the enzyme. The component is not produced by bacteria and is present in the Todd-Hewitt cultivation medium, the beef-heart extract serving primarily as its source.
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Folia Microbiologica, 2001
Preparative isoelectric focusing was used to separate free bacterial NAD+ nucleosidase from its complex with a bound host component. Both fractions were characterized by optimum temperature and activation energy of denaturation. The bacterial product is enzymically inactive. The enzymically active structure is formed upon binding to the host component.
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Preparative isoelectric focusing was used to separate free bacterial NAD+ nucleosidase from its complex with a bound host component. Both fractions were characterized by optimum temperature and activation energy of denaturation. The bacterial product is enzymically inactive. The enzymically active structure is formed upon binding to the host component.
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Die Aktivit�t der NAD-Nucleosidase in verschiedenen Gebieten des Gehirns
Naunyn-Schmiedeberg's Archiv f�r Experimentelle Pathologie und Pharmakologie, 1962openaire +2 more sources
NAD(P) NUCLEOSIDASE OF STREPTOMYCES GRISEUS.
Scientia Sinica, 1996S L, WANG, S C, SHEN
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