Separation of human IgA1 and IgA2 using jacalin-agarose chromatography.

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 micrograms IgA1 and 55.8 micrograms IgA2, 40.3 micrograms IgA1 (80.3% of the original) and 49.6 micrograms 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.

journal_name

J Immunol Methods

authors

Gregory RL,Rundegren J,Arnold RR

doi

10.1016/0022-1759(87)90037-8

subject

Has Abstract

pub_date

1987-05-04 00:00:00

pages

101-6

issue

1

eissn

0022-1759

issn

1872-7905

pii

0022-1759(87)90037-8

journal_volume

99

pub_type

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