Results 121 to 130 of about 3,419 (134)
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A quantitative assay for the cytoplasmic androgen receptor using [3H]dihydrotestosterone in the presence of NAD+-nucleosidase

Acta Endocrinologica, 1983
Abstract. In prostatic cytosol DHT1 is metabolized to 5α-androstane-3α (or β), 17α-diols with a half life of 2 h even at 4°C. Thus, [3H]DHT appears to be a poor marker for a quantitative assessment of androgen receptors (AR). Methyltrienolone (R1881) seems to be advantageous as it is not metabolized.
H, Moeller   +3 more
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Inhibition of nuclear NAD nucleosidase and poly ADP-ribose polymerase activity from rat liver by nicotinamide and 5′-methyl nicotinamide

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 ...
J B, Clark, G M, Ferris, S, Pinder
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Snake venom NAD nucleosidase: Its occurrence in the venoms from the genus Agkistrodon and purification and properties of the enzyme from the venom of A. halys blomhoffii

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.
T, Tatsuki   +3 more
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Streptococcal extracellular NAD+ nucleosidase. Characterization of changes occurring during purification

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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Structural and biochemical basis of NAD+ nucleosidase activity of TIR domain-containing proteins

2021
NAD+ (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).
openaire   +1 more source

Kinetic properties of fractions of extracellular NAD+ nucleosidase fromStreptococcus pyogenes as an example of host selection by a pathogen: Possible role of serum albumin in the organism

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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NAD+ nucleosidase

1991
Dietmar Schomburg, Margit Salzmann
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NAD(P)+ nucleosidase

1991
Dietmar Schomburg, Margit Salzmann
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