Separation of human IgA1 and IgA2 using jacalin-agarose chromatography

Richard L. Gregory, Jan Rundegren, Roland R. Arnold

Research output: Contribution to journalArticle

53 Scopus citations

Abstract

A lectin isolated from the tropical jackfruit, jacalin, previously reported to precipitate human immunoglobulin A (IgA), and conjugated to agarose was used to separate the two subclasses of IgA from secretions. Jacalin-agarose binds specifically to the D-galactose moiety of IgA1 but not to IgA2 which has a different carbohydrate content and structure. IgA2 passed through the jacalin-agarose column and was collected in the void volume. IgA1 was eluted from the lectin by 0.8 M galactose. Of a representative diluted anti-alpha chain-purified colostral IgA preparation containing 50.2 μg IgA1 and 55.8 μg IgA2, 40.3 μg IgA1 (80.3% of the original) and 49.6 μg IgA2 (88.9%) was collected following jacalin-agarose chromatography. The jacalin-purified IgA1 fraction contained 8.0% IgA2 and the IgA2 fraction contained no IgA1. In addition, the IgA1 and IgA2 fractions had naturally occurring antibody activity to a normal oral bacterium. The method is easy, reproducible and specific and has many applications to mucosal immunological investigations.

Original languageEnglish (US)
Pages (from-to)101-106
Number of pages6
JournalJournal of Immunological Methods
Volume99
Issue number1
DOIs
StatePublished - May 4 1987
Externally publishedYes

Keywords

  • IgA1
  • IgA2
  • Jacalin

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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