000			03911nam a22003615i 4500
001			235013
003			ES-VaUE
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007			cr nn 008mamaa
008			150818s2015 xxu| s |||| 0|eng d
020			_a9781493929351
024	7		_a10.1007/978-1-4939-2935-1 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC
245	1	0	_aProtein Arginylation _bMethods and Protocols _cedited by Anna S. Kashina.
250			_a1st edition 2015
264		1	_aNew York, NY _bSpringer International Publishing _c2015
300			_a1 recurso en línea (IX, 149 páginas) _b19 ilustraciones, 11 ilustraciones a color
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 _v1337
505	0		_aProtein Arginylation: Over 50 Years of Discovery -- Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase -- Arginyltransferase: A Personal and Historical Perspective -- Arginylation in a Partially Purified Fraction of 150k xg Supernatants of Axoplasm and Injured Vertebrate Nerves -- Preparation of ATE1 Enzyme from Native Mammalian Tissues -- Correlated Measurement of Endogenous ATE1 Activity on Native Acceptor Proteins in Tissues and Cultured Cells to Detect Cellular Aging -- Assaying the Post-Translational Arginylation of Proteins in Cultured Cells -- Assaying ATE1 Activity in Yeast by β-gal Degradation -- Bacterial Expression and Purification of Recombinant Arginyltransferase (ATE1) and Arg-tRNA Synthetase (RRS) for Arginylation Assays -- Assaying ATE1 Activity In Vitro -- High Throughput Arginylation Assay in Micro plate Format -- Assay of Arginyltransferase Activity by a Fluorescent HPLC Method -- Identification of Arginylated Proteins by Mass Spectrometry -- Analysis of Arginylated Peptides by Subtractive Edman Degradation -- Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles -- Applying Arginylation for Bottom-Up Proteomics -- Development of New Tools for the Studies of Protein Arginylation.
520			_aThis volume presents a comprehensive overview of all the existing methods on analysing protein arginylation, from the early methods utilizing crude protein preparations and whole-cell assays to the latest advanced methods involving recombinant protein techniques, antibodies, high precision mass spectrometry, and chemical probes. This book also includes essays from the founders of the field, who originally discovered arginylation in the early 1960s and brought it to international recognition. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting-edge and thorough, Protein Arginylation: Methods and Protocols would interest the emerging body of scientists involved in the studies of posttranslational arginylation, and the rapidly growing community of researchers working on a broad range of posttranslational modifications, the analysis of which often meets similar challenges and utilizes similar principles as posttranslational arginylation.
700	1		_aKashina, Anna S _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
776	0	8	_iPrinted edition: _z9781493929344
776	0	8	_iPrinted edition: _z9781493929368
776	0	8	_iPrinted edition: _z9781493945689
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-4939-2935-1 _z(usuarios Universidad Europea de Valencia)
942			_2lcc _cLE
988			_aSpringer_Protocols_2015
999			_c235013 _d235013