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020 _a9781592592647
024 7 _a10.1385/1592592643
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
245 1 0 _aProtein Lipidation Protocols
_cedited by Michael H. Gelb.
250 _a1st edition 1999
264 1 _aTotowa, NJ
_bHumana Press
_c1999
300 _a1 recurso en línea (X, 240 páginas)
_b35 ilustraciones
336 _atexto
_btxt
_2rdacontent
337 _aelectrónico
_bc
_2rdamedia
338 _arecurso electrónico
_bcr
_2rdacarrier
347 _aarchivo de texto
_bPDF
490 0 _aMethods in Molecular Biology
_x1940-6029
_v116
505 0 _aIn Vitro Analysis of GPI Biosynthesis in Mammalian Cells -- Selection of Mammalian Cell Mutants in GPI Biosynthesis -- Analysis of the Cell-Surface Distribution of GPI-Anchored Proteins -- Imaging Fluorescence Resonance Energy Transfer as Probe of Membrane Organization and Molecular Associations of GPI-Anchored Proteins -- Purification of Caveolae-Derived Membrane Microdomains Containing Lipid-Anchored Signaling Molecules, Such as GPI-Anchored Proteins, H-Ras, Src-Family Tyrosine Kinases, eNOS, and G-Protein ?-, ?-, and ?-Subunits -- Analysis of Lipids in Caveolae -- Analysis of the Carbohydrate Components of Glycosylphosphatidylinositol Structures Using Fluorescent Labeling -- Analysis of the Lipid Moiety of GPI Anchor in the Yeast Saccharomyces cerevisiae -- Rapid Identification of Cysteine-Linked Isoprenyl Groups by Metabolic Labeling with [3H]Farnesol and [3H]Geranylgeraniol -- Incorporation of Radiolabeled Prenyl Alcohols and Their Analogs into Mammalian Cell Proteins -- Reconstitution of Yeast Farnesyltransferase from Individually Purified Subunits -- Probing the Role of H-Ras Lipidation for Signaling Functions in Xenopus laevis Oocytes -- Fluorescence Measurement of Lipid-Binding Affinity and Interbilayer Transfer of Bimane-Labeled Lipidated Peptides -- Determination of the Kinetics of Intervesicle Transfer and Transbilayer Diffusion of Bimane-Labeled Lipidated Peptides -- Preparation and Assay of Myristoyl-CoA:Protein N-Myristoyltransferase -- Metabolic Labeling of Protein-Derived Lipid Thioesters in Palmitoyl-Protein Thioesterase-Deficient Cells -- Fatty Acid Analysis of Protein-Derived Lipid Thioesters Isolated from Palmitoyl-Protein Thioesterase-Deficient Cells.
520 _aIn Protein Lipidation Protocols, Michael Gelb brings together a collection of readily reproducible techniques for studying protein lipidation, the covalent attachment of lipids to proteins. These cutting-edge methods-many never published before in a "hands-on" format-deal with glycosyl phosphatidylinositol (GPI)-containing compounds, protein fatty acylation, and protein prenylation. Included are novel techniques for determining the chemical structure of GPI-anchors, for radiolabeling the prenyl groups of protein in eukaryotic cells, a tool for developing inhibitors of the protein farnesyltransferase, and for an exciting lysosomal enzyme that cleaves fatty acyl groups from proteins, the first fatty acylase discovered. Protein Lipidation Protocols offers biochemists, cell and molecular biologists, medicinal chemists, and pharmaceutical researchers state-of-the-art tools for understanding the complex biochemistry of protein lipidation, as well as catalyzing the development of many important new biopharmaceuticals, including anticancer drugs.
700 1 _aGelb, Michael H
_eeditor literario
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
776 0 8 _iPrinted edition:
_z9781489943309
776 0 8 _iPrinted edition:
_z9780896035348
776 0 8 _iPrinted edition:
_z9781489943293
856 4 0 _uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592592643
_z(usuarios Universidad Europea de Valencia)
942 _2lcc
_cLE
988 _aSpringer_Protocols_1999
999 _c235389
_d235389