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  • Book
    edited by Kris Gevaert, Joël Vandekerckhove.
    Contents:
    Mass spectrometry-driven proteomics : an introduction / Kenny Helsens [and others]
    Metabolic labeling of model organisms using heavy nitrogen (15N) / Joost W. Gouw, Bastiaan B.J. Tops, and Jeroen Krijgsveld
    Trypsin-catalyzed oxygen-18 labeling for quantitative proteomics / Wei-Jun Qian [and others]
    ICPL labeling strategies for proteome research / Friedrich Lottspeich and Josef Kellermann
    Quantitative proteome analysis using isobaric peptide termini labeling (IPTL) / Magnus Ø. Arntzen [and others]
    Complete chemical modification of amine and acid functional groups of peptides and small proteins / Casey J. Krusemark [and others]
    Production and use of stable isotope-labeled proteins for absolute quantitative proteomics / Dorothée Lebert [and others]
    Organelle proteomics / Sophie Duclos and Michel Desjardins
    Membrane protein digestion
    comparison of LPI HexaLane with traditional techniques / Ping Sui [and others]
    GeLCMS for in-depth protein characterization and advanced analysis of proteomes / Alicia Lundby and Jesper V. Olsen
    Exploring new proteome space : combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics / Nadia Taouatas, Shabaz Mohammed, and Albert J.R. Heck
    Quantitation of newly synthesized proteins by pulse labeling with azidohomoalanine / Gertjan Kramer [and others]
    Analytical strategies in mass spectrometry-based phosphoproteomics / Heidi Rosenqvist, Juanying Ye, and Ole N. Jensen
    Protocol on the use of titanium dioxide chromatography for phosphoproteomics / Martijn W.H. Pinkse, Simone Lemeer, and Albert J.R. Heck
    Positional proteomics at the N-Terminus as a means of proteome simplification / Gemma R. Davidson, Stuart D. Armstrong, and Robert J. Beynon
    N-Terminomics : a high-content screen for protease substrates and their cleavage sites / John C. Timmer and Guy S. Salvesen
    Protease specificity profiling by tandem mass spectrometry using proteome-derived peptide libraries / Oliver Schilling, Ulrich auf dem Keller, and Christopher M. Overall
    Identification of proteolytic products and natural protein N-Termini by terminal amine isotopic labeling of substrates (TAILS) / Alain Doucet [and others]
    Lectins as tools to select for glycosylated proteins / Els J.M. Van Damme
    Strong cation exchange chromatography for analysis of sialylated glycopeptides / Katharina Lohrig, Albert Sickmann, and Urs Lewandrowski
    Titanium dioxide enrichment of sialic acid-containing glycopeptides / Giuseppe Palmisano, Sara E. Lendal, and Martin R. Larsen
    Chemical De-O-glycosylation of glycoproteins for applications in LC-based proteomics / Franz-Georg Hanisch
    Ubiquitination and degradation of proteins / Yelena Kravtsova-Ivantsiv and Aaron Ciechanover
    Bioinformatics challenges in mass spectrometry-driven proteomics / Lennart Martens
    Case study on the comparison of different software tools for automated quantification of peptides / Niklaas Colaert [and others].
    Digital Access Springer 2011
  • Book
    edited by H.-J. Rehm and G. Reed.
    Summary: This reference work describes the state of Biotechnology and serves as a guide to the original literature. It spans the entire field from basic concepts to industrial applications and deals with a wide spectrum of applications. These range from the production of enzymes, biomass, and primary and secondary products of microbial metabolism to the production of foods and feeds, sewage disposal, and other microbial degradations. Volumes 1 and 2 explain the basic concepts of microbial science and bioengineering. The third and fourth volumes describe the industrially important products of microbial metabolism, as well as the production of biomass. The fifth volume deals with the production of foods and feeds with the aid of microbes. Volumes 6A and 6B cover microbial transformations and special microbial processes. Volume 8 deals with biodegradations. The series is intended for microbiologists, biochemists, bioengineers, chemical engineers, and food and pharmaceutical chemists working in industry, academia, and the public sector. A subscription price is available for those signing up for the whole series. Nielsen 9783527257638 20160527

    Contents:
    Introduction
    Characteristics of Industrial Microorganisms
    Growth of Microorganisms
    Basic Metabolic Processes
    Biosynthetic Pathways of Secondary Metabolites in Industrial Microorganisms
    Genetics of Microorganisms in Relation to Industrial Requirements
    Mutations
    Hybridization
    Genetic Engineering
    Sources of Industrial Microorganisms
    Pure Culture Methods for Industrial Microorganisms
    Patent Protection for Biological Inventions
    Batch and Continuous Culture of Microbial Plant and Animal Cells. Nielsen 9783527257638 20160527
    Print 1981-
  • Article
    McPhee D, Pye J, Shortman K.
    Thymus. 1979 Nov;1(3):151-62.
    The DNA of CBA mouse thymocytes was simultaneously labelled with the efficiently reutilized precursor [3H]TdR and the poorly reutilized precursor [125I]UdR, and the subsequent rate of loss of the two thymidine analogues was used to compute the extent of local thymidine reutilization. This should provide a minimum estimate of thymocyte death within the thymus. In agreement with published data, reutilization of thymidine in the "steady state' adult mouse thymus was about 61%. Adrenalectomy was used to show that this turnover was not due to steroid mediated stress effects; nor could it be attributed to direct effects of [125I]UdR itself. Most of the initial uptake and the subsequent turnover was within the major "high theta' thymus subpopulation. A similar study with the growing thymus of 7-day-old mice, when the demand for T cells in the periphery should be high, also revealed a high level (63%) of thymidine reutilization. The results support the view that a minimum of 60% of newly formed thymocytes die within the tyhmus, and that this is a constant and normal aspect of thymus function. This would be compatible with some form of negative selection for the appropriate developing T cells.
    Digital Access Access Options