Related Articles1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of Au(I) and Cu(I) diphosphine complexes on the cell metabolism.
Magn Reson Med. 1991 Mar;18(1):142-58
Authors: Berners-Price SJ, Sant ME, Christopherson RI, Kuchel PW
The effect of the antitumor complex [Au(dppe)2]Cl (where dppe is Ph2P(CH2)2PPh2) on the overall metabolism of cultured mouse L1210 leukemia cells was investigated by comparing 1H and 31P NMR spectra of perchloric acid extracts of cells incubated for 1 h in the presence and absence of 2 microM [Au(dppe)2]Cl. There were marked (ca. two-fold) increases in the levels of lactate and almost all detectable amino acids suggesting a drug-induced increase in the rate of glycolysis and inhibition of protein synthesis. The levels of taurine and phosphorylcholine were significantly decreased and 31P NMR spectra revealed a depletion of nucleoside triphosphates (NTP). The effect on nucleotide metabolism was investigated further by separating purine and pyrimidine nucleotides and precursors by anion-exchange HPLC. NTP levels were depleted by ca. 70-90% and there was a ca. three- to four-fold increase in nucleoside di- and monophosphates. The effect is postulated to be the result of uncoupling of mitochondrial oxidative phosphorylation. The Cu(I) complex [Cu(Ph2PCH = CHPPh2)2]Cl produced a similar effect on the cellular metabolism but was more potent. The water-soluble complex [Cu(Ph2P(CH2)PEt2)2]Cl caused the accumulation of cellular amino acids at a concentration that did not significantly deplete ATP levels.
[NMR paper] Rapid screening of E. coli extracts by heteronuclear NMR.
Rapid screening of E. coli extracts by heteronuclear NMR.
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Curr Protoc Protein Sci. 2003 May;Chapter 7:Unit 7.11
Authors: Gronenborn AM
Assessing whether a protein or protein complex is amenable to structural analysis is an important component in the structural genomics effort. In particular, if complete sets of structures for entire genomes are to be obtained within a reasonable time frame, high throughput methodologies for all steps along the way have to be developed....
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[NMR paper] 1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse
1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse lens.
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Biochim Biophys Acta. 2000 Mar 6;1474(1):23-30
Authors: Nakamura K, Jung YM, Era S, Sogami M, Ozaki Y, Takasaki A
In order to provide new insight into the molecular mechanism of perforating trauma-induced cataract formation in an 8-week-old ddY mouse lens, we performed an in situ investigation into changes in the water-protein and/or...
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[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
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J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
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Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
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[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
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Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
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[NMR paper] Proton NMR studies of the structural and dynamical effect of chemical modification of
Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.
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J Mol Biol. 1994 Nov 4;243(4):719-35
Authors: Roumestand C, Gilquin B,...
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[NMR paper] 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-g
2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-glycero-3-phosphocholine headgroup: a model for transbilayer peptides in surfactant and biological membranes.
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Biochemistry. 1993 Oct 26;32(42):11338-44
Authors: Morrow MR, Taneva S, Simatos GA, Allwood LA, Keough KM
Surfactant protein C (SP-C) was...
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[NMR paper] Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclo
Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclophosphamide metabolites: determination of selective properties of DNA-interstrand and DNA-protein cross-linking mechanisms (alkaline elution and 31P-NMR-spectroscopy) and some aspects of the combination drug and radiotherapy.
Related Articles Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclophosphamide metabolites: determination of selective properties of DNA-interstrand and DNA-protein cross-linking mechanisms (alkaline elution and 31P-NMR-spectroscopy) and...
1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of
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