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1.
J. -E. Augustin G. Cosme F. Couchot B. Dudelzak F. Fulda B. Grelaud G. Grosdidier B. Jean-Marie S. Jullian D. Lalanne V. Lepeltier B. Louis F. Mané C. Paulot R. Riskalla Ph. Roy F. Rumpf G. Szklarz Z. Ajaltouni A. Falvard J. Jousset B. Michel J. C. Montret R. Baldini S. Calcaterra G. Capon D. Bisello G. Busetto S. Limentani M. Nigro L. Pescara M. Posocco P. Sartori L. Stanco DM Collaboration 《Zeitschrift fur Physik C Particles and Fields》1987,36(3):369-376
The radiative decayJ/ψ → γ π+ π? has been studied using the 8.6 millionJ/ψ produced in the DM2 experiment at the DCIe +e? storage rings at Orsay. The π+ π? mass spectrum shows a cleanf 2 (1270) signal, and the possible presence of two other states at thef 2 (1720) andf 4 (2030) masses. For thef 2 (1270), the branching ratio BR(J/ψ →γf)xBR(f→π+ π?) is measured to be (7.50±0.30±1.12)×10?4, and the spin analysis prefers theJ=2 assignment, with helicity parametersx=0.83±0.06 andy=0.01±0.06. The existence of higher mass states is discussed. 相似文献
2.
Ohne Zusammenfassung
Uebersetzt von H. Erbring (Leipzig). 相似文献
3.
The steady propagation of a thin smouldering front in a half-spacehas been considered. A suitable coordinate transformation hasallowed the region near the leading edge of the front to beexamined for both a maintained planar surface and with surfacecollapse due to material shrinkage. The change in the oxidizerconcentration for a small increment in the propagation speedfor large time and surface collapse has been determined. Theinfluence of two types of nonlinear diffusion on the shape ofthe smouldering front has been found; other cases can be dealtwith in a similar manner. 相似文献
4.
5.
Chong BE Yan F Lubman DM Miller FR 《Rapid communications in mass spectrometry : RCM》2001,15(4):291-296
A novel two-dimensional two-column liquid chromatography/mass spectrometry (LC/MS) technique is described in this work, where chromatofocusing (CF) has been coupled to nonporous reversed-phase (NPS-RP) HPLC to separate proteins from human breast epithelial whole cell lysates. The liquid fractions from NPS-RP-HPLC are readily amenable to direct on-line analysis using electrospray ionization orthogonal acceleration time-of-flight mass spectrometry (ESI-TOFMS). A key advantage of this technique is that proteins can be 'peeled off' in the liquid phase from the CF column according to their isoelectric points (pI) in the first chromatographic separation dimension. The NPS-RP-HPLC column further separates these pI-focused fractions based upon protein hydrophobicity as the second chromatographic dimension. The third dimension involves on-line molecular weight determination using ESI-TOFMS. As a result, this method has the potential to be fully automated. In addition, a 2-D protein map of pI versus molecular weight is generated, which is analogous to a 2-D gel image. Thus, this technique may provide a means to study differential expression of proteins from whole cell lysates. 相似文献
6.
Chong BE Lubman DM Rosenspire A Miller F 《Rapid communications in mass spectrometry : RCM》1998,12(24):1986-1993
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) has been used to rapidly profile the protein content of human cell lysates from MCF-10 cell and variant lines. The method was used to study the protein profiles of these cells as they progressed from normal breast epithelium to fully malignant cells. Distinct differences in the protein profiles were observed with progression, and specific proteins associated with carcinogenesis (p53, c-myc, and c-erbB-2) were heavily expressed in these cells as detected by MALDI-TOFMS. These proteins were also isolated using non-porous reversed-phase high performance liquid chromatography (NP-RP-HPLC) and mass analyzed by MALDI-TOFMS to provide molecular weight information without interference from other proteins in the whole cell lysates, and to avoid suppression effects in mixtures of proteins detected by MALDI-TOFMS. In order to confirm the identity of these oncoproteins, the cell lysates were subjected to one-dimensional (1-D) gel separation and subsequently electroblotted onto a poly(vinylidene difluoride) (PVDF) membrane for further analysis. Trypsin and cyanogen bromide digestions were performed on these proteins eluted from excised PVDF bands which were then analyzed by MALDI-TOFMS. The identity of these proteins was confirmed by database matching procedures. 相似文献
7.
A method is developed toward high sequence coverage of proteins isolated from human breast cancer MCF10 cell lines using a 2-D liquid separations. Monolithic-capillary columns prepared by copolymerizing styrene with divinylbenzene are used to achieve high-resolution separation of peptides from protein digests. This separation is performed with minimal sample preparation directly from the 2-D liquid fractionation of the cell lysate. The monolithic column separation is directly interfaced to ESI-TOF MS to obtain a peptide map. The protein digests were also analyzed by MALDI-TOF MS and an accurate M(r) of the intact protein was obtained using an HPLC-ESI-TOF MS. The result is that these techniques provide complementary information where nearly complete sequence coverage of the protein is obtained and can be compared to the experimental M(r) value. The high sequence coverage provides information on isoforms and other post-translational modifications that would not be available from methods that result in low sequence coverage. The results from the use of monolithic columns are compared to that obtained by CE-MS. The monolithic column separations provide a rugged and highly reproducible method for separating protein digests prior to MS analysis and is suited to confidently identify biomarkers associated with cancer progression. 相似文献
8.
D. Bisello G. Busetto A. Castro M. Nigro M. Penzo L. Pescara M. Posocco P. Sartori L. Stanco Z. Ajaltouni A. Falvard J. Jousset B. Michel J. C. Montret A. Antonelli R. Baldini A. Calcaterra G. Capon M. Schioppa J. -E. Augustin G. Cosme F. Couchot B. Dudelzak F. Fulda G. Grosdidier B. Jean-Marie S. Jullian D. Lalanne V. Lepeltier F. Manè C. Paulot R. Riskalla Ph. Roy G. Szklarz DM Collaboration 《Zeitschrift fur Physik C Particles and Fields》1988,39(1):13-19
Thee + e ?→K + K ? cross section has been measured from about 750 events in the energy interval \(1350 \leqq \sqrt s \leqq 2400 MeV\) with the DM2 detector at DCI. TheK ± form factor |F F ±| cannot be explained by the ρ, ω, ? and ρ′(1600). An additional resonant amplitude at 1650 MeV has to be added as suggested by a previous experiment. 相似文献
9.
10.
Wall DB Kachman MT Gong SS Parus SJ Long MW Lubman DM 《Rapid communications in mass spectrometry : RCM》2001,15(18):1649-1661
A liquid-phase three-dimensional protein separation method has been developed that is used to separate the cytosolic fraction of a HEL cell lysate via isoelectric focusing (IEF), nonporous silica (NPS) reversed-phase high-performance liquid chromatography (RP-HPLC) and electrospray ionization time-of-flight mass spectrometry (ESI-TOFMS), respectively. Several hundred unique protein molecular weights were observed in a pI range from 4.8 to 8.5 and a mass range from 5 to 85 kDa. Proteins were positively identified by analysis of the pI (+/-0.5 pI units), an intact protein molecular weight (+/-150 ppm), and peptide mass mapping results. Using the molecular weight (MW) and peptide mapping results of identified proteins it was possible to characterize their posttranslational (PTMs) and/or sequence modifications. PTMs were detected on both forms of cytosolic actin, heat shock 90 beta, HINT and alpha-enolase. Sequence modifications or conflicts were observed for beta-and gamma-actin, ATP beta-synthase and heat shock 90 beta. IEF-NPS-RP-HPLC/ESI-TOFMS was used to determine experimental pI, MW and relative hydrophobicity values for each protein detected. This data was used to generate a 2-D pI-MS protein map, where proteins are displayed according to their pI and molecular weight. Protein molecular weight peaks are represented as bands in the 2-D pI-MS image where the gray scale of each band is proportional to the intensity of the protein molecular weight peak. In addition, a third hydrophobicity dimension (%B) was added as the % acetonitrile elution to generate a 3-D pI-MS-%B plot where each protein can be tagged according to three parameters. 相似文献