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Attomole protein characterization by capillary electrophoresis-mass spectrometry (1996)

G. A. Valaskovic ; N. L. Kelleher ; F. W. McLafferty

American Association for the Advancement of Science (AAAS)

In: Science. 273(5279): 1199-202.

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Publikationsdatum: 1996-08-30

Beschreibung: Electrospray ionization with an ultralow flow rate (〈/=4 nanoliters per minute) was used to directly couple capillary electrophoresis with tandem mass spectrometry for the analysis and identification of biomolecules in mixtures. A Fourier transform mass spectrometer provided full spectra (〉30 kilodaltons) at a resolving power of approximately 60,000 for injections of 0.7 x 10(-18) to 3 x 10(-18) mole of 8- to 29-kilodalton proteins with errors of 〈1 dalton in molecular mass. Using a crude isolate from human blood, a value of 28,780.6 daltons (calculated, 28,780.4 daltons) was measured for carbonic anhydrase, representing 1 percent by weight of the protein in a single red blood cell. Dissociation of molecular ions from 9 x 10(-18) mole of carbonic anhydrase gave nine sequence-specific fragment ions, more data than required for unique retrieval of this enzyme from the protein database.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valaskovic, G A -- Kelleher, N L -- McLafferty, F W -- 08-T2GM07273/GM/NIGMS NIH HHS/ -- GM16609/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1199-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703047" target="_blank"〉PubMed〈/a〉

Schlagwort(e): Animals ; Carbonic Anhydrases/*analysis/chemistry ; Cattle ; Cytochrome c Group/analysis/chemistry ; Electrophoresis, Capillary/*methods ; Horses ; Humans ; Mass Spectrometry/*methods ; Molecular Weight ; Proteins/*analysis/chemistry ; Sensitivity and Specificity ; Spectroscopy, Fourier Transform Infrared ; Ubiquitins/analysis/chemistry

Print ISSN: 0036-8075

Digitale ISSN: 1095-9203

Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik

Publiziert von American Association for the Advancement of Science (AAAS)

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Blocked Ras activation in anergic CD4+ T cells (1996)

P. E. Fields ; T. F. Gajewski ; F. W. Fitch

American Association for the Advancement of Science (AAAS)

In: Science. 271(5253): 1276-8.

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Publikationsdatum: 1996-03-01

Beschreibung: T cell anergy is a state of functional unresponsiveness characterized by the inability to produce interleukin-2 (IL-2) upon T cell receptor stimulation. The mitogen-activated protein kinases ERK-1 and ERK-2 and the guanosine triphosphate-binding protein p21ras were found to remain unactivated upon stimulation of anergic murine T helper cell 1 clones. The inability to activate the Ras pathway did not result from a defect in association among Shc, Grb-2, and murine Son of Sevenless, nor from a defect in their tyrosine phosphorylation. This block in Ras activation may lead to defective transactivation at activator protein 1 sites in anergic cells and may enable T cells to shut down IL-2 production selectively during anergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fields, P E -- Gajewski, T F -- Fitch, F W -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1276-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute, Department of Pathology, University of Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638108" target="_blank"〉PubMed〈/a〉

Schlagwort(e): *Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD4/immunology ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Clonal Anergy ; Clone Cells ; GRB2 Adaptor Protein ; Guanine Nucleotide Exchange Factors ; Guanosine Triphosphate/metabolism ; Interleukin-2/biosynthesis ; Ionomycin/pharmacology ; Lymphocyte Activation ; Mice ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Protein-Tyrosine Kinases/metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Antigen, T-Cell/immunology ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Th1 Cells/*immunology/metabolism ; ras Guanine Nucleotide Exchange Factors

Print ISSN: 0036-8075

Digitale ISSN: 1095-9203

Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik

Publiziert von American Association for the Advancement of Science (AAAS)

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Structure in Thin and Ultrathin Spin-Cast Polymer Films (1996)

C. W. Frank ; V. V. Rao ; M. M. Despotopoulou ; [weitere]

American Association for the Advancement of Science (AAAS)

In: Science. 273(5277): 912-5.

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Publikationsdatum: 1996-08-16

Beschreibung: The molecular organization in ultrathin polymer films (thicknesses less than 1000 angstroms) and thin polymer films (thicknesses between 1000 and 10,000 angstroms) may differ substantially from that of bulk polymers, which can lead to important differences in resulting thermophysical properties. Such constrained geometry films have been fabricated from amorphous poly(3-methyl-4-hydroxy styrene) (PMHS) and semicrystalline poly(di-n-hexyl silane) (PD6S) by means of spin-casting. The residual solvent content is substantially greater in ultrathin PMHS films, which suggests a higher glass transition temperature that results from a stronger hydrogen-bonded network as compared with that in thicker films. Crystallization of PD6S is substantially hindered in ultrathin films, in which a critical thickness of 150 angstroms is needed for crystalline morphology to exist and in which the rate of crystallization is initially slow but increases rapidly as the film approaches 500 angstroms in thickness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frank -- Rao V -- Despotopoulou -- Pease -- Hinsberg -- Miller -- Rabolt -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉C. W. Frank, V. Rao, and M. M. Despotopoulou are in the Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA. R. F. W. Pease is in the Department of Electrical Engineering, Stanford University, Stanford, CA 94305, USA. W. D. Hinsberg, R. D. Miller, and J. F. Rabolt are at the IBM Almaden Research Center, IBM Research Division, 650 Harry Road, San Jose, CA 95120-6099, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688068" target="_blank"〉PubMed〈/a〉

Print ISSN: 0036-8075

Digitale ISSN: 1095-9203

Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik

Publiziert von American Association for the Advancement of Science (AAAS)

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