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Pichia Protocols Second Edition 2007 [Kõva köide]

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  • Formaat: Hardback, 268 pages, kõrgus x laius: 229x152 mm, kaal: 588 g, XII, 268 p., 1 Hardback
  • Sari: Methods in Molecular Biology 389
  • Ilmumisaeg: 08-Aug-2007
  • Kirjastus: Humana Press Inc.
  • ISBN-10: 1588294293
  • ISBN-13: 9781588294296
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  • Formaat: Hardback, 268 pages, kõrgus x laius: 229x152 mm, kaal: 588 g, XII, 268 p., 1 Hardback
  • Sari: Methods in Molecular Biology 389
  • Ilmumisaeg: 08-Aug-2007
  • Kirjastus: Humana Press Inc.
  • ISBN-10: 1588294293
  • ISBN-13: 9781588294296
Teised raamatud teemal:
Pichia pastoris is a recombinant protein production system that was described in the 1998 first edition. This second edition is intended to be not so much a replacement of the first as an extension, focusing on information that has emerged over the past decade, particularly the increased range of proteins that can be made in useful amounts using the system. Researchers set out laboratory procedures step-by-step for such activities as saturating the secretory pathway by over-expressing a hookworm protein, and the heavy labeling of recombinant proteins. Annotation ©2008 Book News, Inc., Portland, OR (booknews.com)

Pichia Protocols focuses on recent developments of Pichia pastoris as a recombinant protein production system. Highlighted topics include a discussion on the use of fermentors to grow Pichia pastoris, information on the O- and N-linked glycosylation, methods for labeling Pichia pastoris expressed proteins for structural studies, and the introduction of mutations in Pichia pastoris genes by the methods of restriction enzyme-mediated integration (REMI).This volume fully updates and expands upon the first edition of Pichia Protocols, and focuses primarily on information that has come to light since its original publication. Each chapter presents cutting-edge and cornerstone protocols for utilizing P. pastoris as a model recomibinant protein production system.

This book focuses on recent developments of Pichia pastoris as a recombinant protein production system. The volume fully updates and expands upon the first edition, and focuses primarily on information that has come to light since its original publication. Highlighted topics include a discussion on the use of fermentors to grow Pichia pastoris, information on the O- and N-linked glycosylation, methods for labeling Pichia pastoris expressed proteins for structural studies, and the introduction of mutations in Pichia pastoris genes by the methods of restriction enzyme-mediated integration (REMI).Each chapter presents cutting-edge and cornerstone protocols for utilizing P. pastoris as a model recomibinant protein production system.

Arvustused

From the reviews of the second edition:









"P. pastoris has many superior traits. can grow to very high cell densities prior to switching on an inducible promoter (the AOX1 gene) for maximal recombinant protein production. The diversity of such proteins produced by expression strains of P. pastoris is quite amazing and this book describes detailed experimental protocols for a few of them (e.g. hookworm protein, botulinum toxin). This is a stand-alone book . a book that will prove valuable to yeast molecular geneticists and biotechnologists." (Graeme Walker, Microbiology Today, May, 2008)

Preface v
Contributors ix
Introduction: Distinction Between Pichia pastoris and Other Expression Systems
1(10)
James M. Cregg
Vectors and Strains for Expression
11(16)
Joan Lin-Cereghino
Geoff P. Lin-Cereghino
DNA-Mediated Transformation
27(16)
James M. Cregg
Rational Design and Optimization of Fed-Batch and Continuous Fermentations
43(22)
Wenhui Zhang
Mehmet Inan
Michael M. Meagher
Saturation of the Secretory Pathway by Overexpression of a Hookworm (Necator americanus) Protein (Na-ASP1)
65(12)
Mehmet Inan
Sarah A. Fanders
Wenhui Zhang
Peter J. Hotez
Bin Zhan
Michael M. Meagher
Purification of the N- and C-Terminal Subdomains of Recombinant Heavy Chain Fragment C of Botulinum Neurotoxin Serotype C
77(22)
Jicai Huang
Rick Barent
Mehmet Inan
Mark Gouthro
Virginia P. Roxas
Leonard A. Smith
Michael M. Meagher
Rapid Screening of Chromatography Resins for the Purification of Proteins
99(8)
Sandra E. Rios
Erin M. Giaccone
Tillman U. Gerngross
Characterization of O-Linked Saccharides on Glycoproteins
107(12)
Roger K. Bretthauer
Modification of the N-Glycosylation Pathway to Produce Homogeneous Human-Like Glycans Using GlycoSwitch Plasmids
119(20)
Wouter Vervecken
Nico Callewaert
Vladimir Kaigorodov
Steven Geysens
Roland Contreras
N-Linked Glycan Characterization of Heterologous Proteins
139(12)
Huijan Li
Robert G. Miele
Teresa I. Mitchell
Tillman U. Gerngross
Heavy Labeling of Recombinant Proteins
151(14)
Eric Rodriguez
Selenomethionine Labeling of Recombinant Proteins
165(10)
Anna M. Larsson
T. Alwyn Jones
Selective Isotopic Labeling of Recombinant Proteins Using Amino Acid Auxotroph Strains
175(14)
James W. Whittaker
Classical Genetics
189(14)
Ilya Tolstorukov
James M. Cregg
Identification of Pexophagy Genes by Restriction Enzyme-Mediated Integration
203(16)
Laura A. Schroder
Benjamin S. Glick
William A. Dunn, Jr.
Characterization of Protein--Protein Interactions: Application to the Understanding of Peroxisome Biogenesis
219(20)
Sebastien Leon
Ivet Suriapranata
Mingda Yan
Naganand Rayapuram
Amar Patel
Suresh Subramani
Localization of Proteins and Organelles Using Fluorescence Microscopy
239(12)
Jean-Claude Farre
Kanae Shirahama-Noda
Lan Zhang
Keith Booher
Suresh Subramani
Fluorescence Microscopy and Thin-Section Electron Microscopy
251(10)
Benjamin S. Glick
Index 261