Elimination of undesirable immunoglobulin contaminants including aggregated IgG from γ-globulin preparations by jackfruit lectin affinity chromatography

Kondoh, Hozumi; Kobayashi, Kunihiko

doi:10.1016/0009-8981(88)90363-4

Cited by 11 publications

(2 citation statements)

References 8 publications

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“…In contrast, although they observed a similar specificity with JCE from seeds collected in the Philippines, Kondoh et al (8) found positive reactions by gel double-diffusion between a half-purified jackfruit seed preparation from Okinawa and IgM, IgA2m(2), and IgE (in addition to precipitation with IgA 1 and IgD); later on, these same authors reported the reactivity of IgA2 of both allotypes, IgM, IgE, and even aggregated IgG with a preparation from a peculiar batch of jackfruit seeds that were "rounder and thicker in shape" than others (18). It was suggested that these differences might reflect variations of the properties of jacalin according to the geographic origin of the jackfruit seeds.…”

Section: Carbohydrate Specificitymentioning

confidence: 99%

Jacalin: A new laboratory tool in immunochemistry and cellular immunology

Aucouturier

Pineau

Brugier

et al. 1989

Clinical Laboratory Analysis

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In recent years, a new lectin--jacalin--has raised the interest of immunologists because of its original properties with respect to human immunoglobulins and lymphocytes. Its structure and carbohydrate binding specificity are now well documented, and it can be purified easily from jackfruit seeds by ion exchange or affinity chromatography. The binding and precipitating specificities of jacalin with heavy chains of human immunoglobulins allow its use as a diagnostic (IgA subclass typing) and preparative tool (purification of IgA and IgD, removal of IgA from biologic samples and preparations). Other possible applications of jacalin's binding properties also can be envisaged. In addition, the lectin displays a mitogenic activity specific for human CD4 T-lymphocytes; consequently, the proliferative response induced by jacalin appears to represent a new and interesting assay for a functional study of CD4 cells, with obvious applications in primary and acquired, especially AIDS, immune deficiency states.

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Section: Carbohydrate Specificitymentioning

confidence: 99%

Jacalin: A new laboratory tool in immunochemistry and cellular immunology

Aucouturier

Pineau

Brugier

et al. 1989

Clinical Laboratory Analysis

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“…The two oligosaccharides in the Fc region of normal serum IgG are buried between the two CH2 domains and highly conserved (50). In fact, it was reported that some plant lectins did not react with normal IgG but became reactive with the IgG after heat aggregation, indicating that alteration of IgG tertiary structure by denaturation lead the carbohydrate moiety to become accessible to the lectins (51). It thus could be assumed that IgG-G 0 of the RA patients but not of normal individuals has altered tertiary structure with exposed carbohydrate moiety.…”

Section: Figurementioning

confidence: 99%

Degalactosylated and/or Denatured IgA, but Not Native IgA in Any Form, Bind to Mannose-Binding Lectin

Terai

Kobayashi

Vaerman

et al. 2006

The Journal of Immunology

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Mannose-binding lectin (MBL) is reported to bind to agalactosyl IgG, but not to normally galactosylated (native) IgG. It was recently reported that serum polymeric IgA in its native form reacts with MBL, whereas a more recent report has claimed that native IgD and IgE, and possibly IgM, do not. This led us to investigate whether IgA is truly reactive with MBL. To accomplish this, we collected purified human Igs, of various classes, subclasses, and allotypes, and tested their ability to bind to MBL using an ELISA method. Among these preparations, only one (monoclonal IgA2m(2):Kur) exhibited significant MBL binding. In particular, polymeric or monomeric forms of our normal serum IgA preparation lacked any ability to bind to MBL whatsoever. However, all the Ig preparations which had not bound to MBL became able to do so when they were degalactosylated with a galactosidase treatment, and the binding was further enhanced by acidic denaturation of the Igs. Among the degalactosylated and/or acid-denatured IgA, the IgA2 subclass exhibited a higher level of MBL binding than did IgA1. Our results suggest that MBL does not bind to native Igs (viewed in principle as “self” components), and that only Igs with abnormal glycosylation (degalactosylated forms) and/or denaturation would be MBL reactive.

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