Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A.

Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Abstract Text:

    Papain digestion of porcine IgG in the absence of cysteine resulted in a rather poor yield of fragments (less than 5 per cent). In the presence of cysteine, 70 to 80 per cent of the IgG was degradated in 4 h. Fragments with molecular weight of about 100,000 and 50,000 were separated by gel filtration. The minor fraction (mol. wt. 100,000) most probably consisted of F(c)2 fragments. Fab/c fragments with both Fc and Fab determinants, and also probably some F(ab)2-like fragments. The F(c)2 fragments appeared to be a dimer of Fc stabilized by disulphide bonds. The second main fraction (mol. wt. 50,000) contained Fc and Fab fragments. Mild reduction of the Fc fragments resulted in Fc subfragments of different sizes, thus indicating that papain cleavages had occurred on different spots in the Fc chain. Non-reduced Fc fragments therefore seem to consist of several Fc subfragments stabilized by disulphide bonds. The protein A reactivity of the isolated Fc fragments were rather low compared to the reactivity of intact IgG, respectively 5--15 and 90 per cent. In addition, protein A reactive Fab fragments were isolated from normal porcine IgG.

    Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Publishing Authors By Initials

    For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

    PUBMED ID PMID:

    MEDLINE DATE:

    Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Acta pathologica et microbiologica Scandinavica. S

    VOLUME: 87C

    Page Numbers: 177-83

    Journal Abbreviation:

    ISSN: 0304-1328

    DAY: 26

    MONTH: Jun

    YEAR: 1979

    Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7508469

    Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Keywords Mesh Terms:

    KEYWORDS: Swine

    MESH TERMS: immunology

    Chemical & Substance for Abstract: Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A. Information

    Substance Name: Papain

    Registry Number: EC 3.4.22.2

    Grant and Affiliation Information for Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A.

    AFFILIATION:

    Country: DENMARK

    DENMARK Research PublicationDENMARK Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Acta Pathol Microbiol Scand [C

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News