Zobrazeno 1 - 10
of 23
pro vyhledávání: '"L P, Solomonson"'
Publikováno v:
Biochimica et biophysica acta. 1382(1)
A water soluble truncated heme domain (a tetramer of MW = 45 kDa) of the tetrameric nitrate reductase complex from the green alga Chlorella vulgaris has been overexpressed and purified. This truncated heme domain with four identical subunits has a hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7efb045eac346c4ae6b281b7554dc8e2
https://pubmed.ncbi.nlm.nih.gov/9507089
https://pubmed.ncbi.nlm.nih.gov/9507089
Publikováno v:
The Journal of biological chemistry. 268(5)
A recombinant protein corresponding to the putative heme-binding domain of assimilatory NADH:nitrate reductase from Chlorella vulgaris has been expressed and purified from transformed Escherichia coli BL21 cells. The recombinant protein, exhibited a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::62b658db549965ece93b081a18b59cfb
https://pubmed.ncbi.nlm.nih.gov/8429004
https://pubmed.ncbi.nlm.nih.gov/8429004
Autor:
L P, Solomonson
Publikováno v:
The Journal of the Florida Medical Association. 78(2)
Nitric oxide (NO) has been identified as a naturally-occurring metabolite in mammalian systems, formed from the amino acid arginine in response to a variety of physiological stimuli. It appears to function in cell-cell communication and may act eithe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0275b107b6fc941bb9c110771636a288
https://pubmed.ncbi.nlm.nih.gov/2026996
https://pubmed.ncbi.nlm.nih.gov/2026996
Molybdenum sites of Escherichia coli and Chlorella vulgaris nitrate reductase: a comparison by EXAFS
Publikováno v:
Journal of the American Chemical Society. 106:1467-1471
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5635036079de1b344d32dd6104a01c4a
https://doi.org/10.1021/ja00317a047
https://doi.org/10.1021/ja00317a047
Autor:
L P, Solomonson, P R, Halabrin
Publikováno v:
Cancer research. 41(2)
Adriamycin ws tested as a possible inhibitor of cardiac sodium-potassium-activated adenosine triphosphatase (Na-K-ATPase). At concentrations of 10(-4) M and lower, Adriamycin had no effect upon either ouabain-sensitive (Na-K-ATPase) or ouabain-insens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::492a08df7f6bf759e0056d1f3cefd2f8
https://pubmed.ncbi.nlm.nih.gov/6256069
https://pubmed.ncbi.nlm.nih.gov/6256069
Publikováno v:
Biochemistry. 27(16)
Oxidation-reduction midpoint potentials for flavin, heme, and molybdenum-pterin prosthetic groups of assimilatory nitrate reductase (NR) from Chlorella vulgaris were measured at room temperature by using CD and EPR potentiometry. The CD changes accom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::43b9235a28e773339a754b72a4648e23
https://pubmed.ncbi.nlm.nih.gov/2847786
https://pubmed.ncbi.nlm.nih.gov/2847786
Autor:
L P, Solomonson, M J, McCreery
Publikováno v:
The Journal of biological chemistry. 261(2)
Assimilatory NADH:nitrate reductase from Chlorella is a homotetramer which contains one of each of the prosthetic groups FAD, heme, and Mo6+ per 100-kDa subunit. At low protein concentrations, this tetramer dissociates to a fully active dimer. To fur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::60eaac59aaaf75d3997fb3d67f9daca6
https://pubmed.ncbi.nlm.nih.gov/3510207
https://pubmed.ncbi.nlm.nih.gov/3510207
Autor:
W D, Howard, L P, Solomonson
Publikováno v:
The Journal of biological chemistry. 257(17)
Gel chromatography experiments over a wide range of protein concentrations showed that Chlorella nitrate reductase is a nonassociating protein with a Stokes radius of 81 A. Sedimentation equilibrium of nitrate reductase in H2O-D2O solvents yielded a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fdf17882c0649bee14377cc37261b108
https://pubmed.ncbi.nlm.nih.gov/7202004
https://pubmed.ncbi.nlm.nih.gov/7202004
Publikováno v:
The Journal of biological chemistry. 261(24)
Assimilatory nitrate reductase from Chlorella is a homotetramer which contains one of each of the prosthetic groups FAD, heme, and molybdenum per subunit. Besides the reduction of nitrate by NADH, nitrate reductase also catalyzes the partial activiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d4deee9bccaa60abe1bd9980e4bc0498
https://pubmed.ncbi.nlm.nih.gov/3015963
https://pubmed.ncbi.nlm.nih.gov/3015963
Autor:
W D, Howard, L P, Solomonson
Publikováno v:
The Journal of biological chemistry. 256(24)
Chlorella nitrate reductase catalyzes the reduction of nitrate to nitrite by NADH. Initial velocity studies showed that the kinetic mechanism is sequential, indicating that both substrates must bind to the enzyme before any products are released. Pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d41ca3cbc67f440cab61be10da755c20
https://pubmed.ncbi.nlm.nih.gov/6273405
https://pubmed.ncbi.nlm.nih.gov/6273405