Results 121 to 129 of about 70,171 (129)
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Activation of calmodulin-dependent NAD+ kinase by trypsin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Sea 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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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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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
1971Publisher 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, 1967IN 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, 2000Measurable 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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Plant NAD Kinase: Regulation by Calcium and Calmodulin [PDF]
, 1986 It has been shown that illumination of plant seedlings or plant tissues causes an increase of NADP and a decrease of NAD (Muto et al., 1981). So far, NAD kinase (AMP:NAD 2′- phosphotransferase; EC 2.7.1.23) has been the only enzyme which is known to catalyzes the phosphorylation of NAD to NADP.
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INVESTIGATION OF CALMODULIN‐REGULATED NAD KINASE IN PROLIFERATING FIBROBLASTS*
Annals of the New York Academy of Sciences, 1980Martina L. Veigl, Thomas C. Vanaman
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