We are analyzing https://link.springer.com/protocol/10.1007/978-1-60327-310-7_15.

Title:
Use of Sequential Chemical Extractions to Purify Nuclear Membrane Proteins for Proteomics Identification | SpringerLink
Description:
The nuclear envelope (NE) is a double membrane system that is both a part of the endoplasmic reticulum and part of the nucleus. As its constituent proteins tend to be highly complexed with nuclear and cytoplasmic components, it is notoriously difficult to purify. Two...
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(2000) Membrane proteins and proteomics: an amour impossible?

Schema {🗺️}

ScholarlyArticle:
      headline:Use of Sequential Chemical Extractions to Purify Nuclear Membrane Proteins for Proteomics Identification
      pageEnd:225
      pageStart:201
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-60327-310-7.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Membrane Proteomics
         isbn:
            978-1-60327-310-7
            978-1-60327-309-1
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Nadia Korfali
            affiliation:
                  name:University of Edinburgh
                  address:
                     name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Elizabeth A.L. Fairley
            affiliation:
                  name:University of Edinburgh
                  address:
                     name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Selene K. Swanson
            affiliation:
                  name:The Stowers Institute for Medical Research
                  address:
                     name:The Stowers Institute for Medical Research, Kansas City, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Laurence Florens
            affiliation:
                  name:The Stowers Institute for Medical Research
                  address:
                     name:The Stowers Institute for Medical Research, Kansas City, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Eric C. Schirmer
            affiliation:
                  name:University of Edinburgh
                  address:
                     name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Nuclear envelope (NE), endoplasmic reticulum (ER), microsomal membrane (MM), integral membrane protein, inner nuclear membrane (INM), outer nuclear membrane (ONM), detergent, chaotrope, alkaline, multidimensional protein identification technology (MudPIT)
      description:The nuclear envelope (NE) is a double membrane system that is both a part of the endoplasmic reticulum and part of the nucleus. As its constituent proteins tend to be highly complexed with nuclear and cytoplasmic components, it is notoriously difficult to purify. Two methods can reduce this difficulty for the identification of nuclear membrane proteins: comparison to contaminating membranes and chemical extractions to enrich for certain groups of proteins. The purification of nuclear envelopes and contaminating microsomal membranes is described here along with procedures for chemical extraction using salt and detergent, chaotropes, or alkaline solutions. Each extraction method enriches for different combinations of nuclear envelope proteins. Finally, we describe the analysis of these fractions with MudPIT, a proteomics methodology that avoids gel extraction of bands to facilitate identification of minor proteins and membrane proteins that do not resolve well on gels. Together these three approaches can significantly increase the output of proteomics studies aimed at identifying the protein complement of subcellular membrane systems.
      datePublished:2009
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Book:
      name:Membrane Proteomics
      isbn:
         978-1-60327-310-7
         978-1-60327-309-1
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Edinburgh
      address:
         name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
         type:PostalAddress
      name:University of Edinburgh
      address:
         name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
         type:PostalAddress
      name:The Stowers Institute for Medical Research
      address:
         name:The Stowers Institute for Medical Research, Kansas City, USA
         type:PostalAddress
      name:The Stowers Institute for Medical Research
      address:
         name:The Stowers Institute for Medical Research, Kansas City, USA
         type:PostalAddress
      name:University of Edinburgh
      address:
         name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Nadia Korfali
      affiliation:
            name:University of Edinburgh
            address:
               name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
               type:PostalAddress
            type:Organization
      name:Elizabeth A.L. Fairley
      affiliation:
            name:University of Edinburgh
            address:
               name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
               type:PostalAddress
            type:Organization
      name:Selene K. Swanson
      affiliation:
            name:The Stowers Institute for Medical Research
            address:
               name:The Stowers Institute for Medical Research, Kansas City, USA
               type:PostalAddress
            type:Organization
      name:Laurence Florens
      affiliation:
            name:The Stowers Institute for Medical Research
            address:
               name:The Stowers Institute for Medical Research, Kansas City, USA
               type:PostalAddress
            type:Organization
      name:Eric C. Schirmer
      affiliation:
            name:University of Edinburgh
            address:
               name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
               type:PostalAddress
            type:Organization
PostalAddress:
      name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
      name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
      name:The Stowers Institute for Medical Research, Kansas City, USA
      name:The Stowers Institute for Medical Research, Kansas City, USA
      name:The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, University of Edinburgh, Edinburgh, UK
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