title: Isolation of IgA1 from human serum by affinity chromatography using an immobilized extract of the albumin gland of Helix pomatia.
abstract: An extract of the albumin gland of Helix pomatia was linked to Sepharose-4B and used to prepare IgA from group O human serum; immunoelectrophoresis showed that the preparation was free of IgG and IgM. From studies with specific IgA subclass antisera and by comparison with the activity of jacalin-produced material the Helix pomatia extract was found to be IgA1 specific. The preparation had red cell anti-A, B specificity and was suitable for standardizing and controlling anti-human IgA reagents. Preparations using six different carbohydrates as eluants inhibited the agglutination reaction between anti-human IgA and IgA-coated red cells to varying degrees. The pattern of reactions suggested that N-acetyl glucosamine was the IgA binding site for Helix pomatia; this differed from its blood group A determinant (N-acetyl galactosamine) which was the same as that for the IgA1 reactive component of jacalin.
authors.affiliation: Trent Regional Blood Transfusion Centre, Sheffield, U.K.
authors.forename: J R
authors.initials: JR
authors.lastname: Booth
authors.forename: R
authors.initials: R
authors.lastname: Munks
authors.forename: R J
authors.initials: RJ
authors.lastname: Sokol
mesh_terms: D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity; D005260:Female; D006372:Helix, Snails / Q000276:immunology*; D006801:Humans; D007070:Immunoglobulin A / Q000276:immunology / Q000302:isolation & purification*; D037102:Lectins / Q000276:immunology*; D037121:Plant Lectins
chemical_list: C038095:Helix lectin; D007070:Immunoglobulin A; D037102:Lectins; D037121:Plant Lectins; C043696:jacalin