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Developmental Ontogeny of NAD+ Kinase in the Rat Conceptus

Toxicology and Applied Pharmacology, 2001
The ubiquitous NAD+ kinase (NADK) is the only known enzyme to catalyze formation of NADP+ from NAD+. The capacity to maintain an adequate supply of NADP(H) has important implications for development because of its requirement as a cofactor and electron donor in biosynthesis and detoxication reactions.
Surekha S. Akella, Craig Harris
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PROPERTIES OF RAT BRAIN NAD‐KINASE

Journal of Neurochemistry, 1970
Abstract— NAD‐kinase was purified from rat brain acetone powder according to the method of Wang and Kaplan (1954). The acetate buffer supernatant showed only very low specific activity but was largely free of the factors that interfere with the enzyme assay. The Michaelis constants for both substrates were determined, the values were 0·5 mm for NAD and
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Developmental regulation of NAD+ kinase in Neurospora crassa

Archives of Microbiology, 1982
The specific activity of NAD+ kinase (ATP:NAD+ 2'-phosphotransferase, EC 2.7.1.23) from Neurospora crassa shows sharp peaks when the organism enters a new developmental stage of the asexual life cycle: the peaks are observed during hydration and germination of conidia, at the transition from exponential to stationary growth and at the photostimulated ...
Mikhail S. Kritsky   +3 more
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Production of NADP by immobilized cells with NAD kinase

Biotechnology and Bioengineering, 1982
AbstractBy the radiation‐copolymerization method with polyethylene glycoldimethacrylate (PGD) as a main polymerizable reagent, microbial cells of Brevibacterium ammoniagenes were immobilized with high specific activity of NAD kinase and high mechanical strength.
Toshio Watanabe   +4 more
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Structural and Functional Characterization of Human NAD Kinase

Biochemical and Biophysical Research Communications, 2001
NADP is essential for biosynthetic pathways, energy, and signal transduction. Its synthesis is catalyzed by NAD kinase. Very little is known about the structure, function, and regulation of this enzyme from multicellular organisms. We identified a human NAD kinase cDNA and the corresponding gene using available database information.
Felicitas Lerner   +3 more
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Activation of calmodulin-dependent NAD+ kinase by trypsin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
Sea urchin egg NAD+ kinase (ATP:NAD+ 2'-phosphotransferase, EC 2.7.1.23), a calmodulin-dependent enzyme, can be activated by a moderate treatment with trypsin in a similar fashion to calmodulin. Stimulation by trypsin is dependent on its concentration (half-maximal dose: 1.5 microgram/ml) but independent of the presence of calcium.
Pierre Guerrier, Laurent Meijer
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Crystallographic Studies of Mycobacterium tuberculosis Polyphosphate/ATP-NAD Kinase Complexed with NAD

Journal of Bioscience and Bioengineering, 2004
NAD kinase from Mycobacterium tuberculosis (Ppnk) uses ATP or inorganic polyphosphate [poly(P)]. Ppnk overexpressed in Escherichia coli was purified and crystallized in the presence of NAD. Preliminary X-ray analysis of the resultant crystal indicate that the crystal belongs to hexagonal space group P6(2)22 and is holo-Ppnk complexed with NAD.
Kousaku Murata   +7 more
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[119] NAD+ kinase in liver tissue

1971
Publisher Summary This chapter discusses the assay method, purification procedure, and properties of the enzyme nicotinamide adenine dinucleotide (NAD + ) kinase in frozen rat and calf liver tissue. The nicotinamide adenine dinucleotide phosphate (NADP + ) formed in the reaction mixture is assayed by method based on the measurement of the change in ...
I.L. Yero, L.S. Dietrich
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Effect of Methotrexate on NAD Kinase Activity in Leukaemic Mice

Nature, 1967
IN the course of treatment of leukaemia L1210 in mice using an antifolate compound, methotrexate (MTX), the leukaemic cells are affected early during treatment and later, while becoming resistant1, show impaired retention and decreased permeability to the drug2–4.
Mhatre, R M   +2 more
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ATP- and polyphosphate-dependent bacterial NAD+ kinases

Applied Biochemistry and Microbiology, 2000
Measurable levels of activity of NAD+ kinases of actinomycetesMicrococcus luteus andCoryne-bacterium ammoniagenes were observed after substituting inorganic tripolyphosphate for ATP, whereas the enzyme from the eubacteriumEscherichia coli was not active with this substrate. Gradient PAGE found two molecular isoforms of NAD+ kinase inC.
Afanas'eva Tp   +3 more
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