Binding of mammalian β2-microglobulin by glycoproteins in fish serum

Lögdberg, Lennart; Björck, Lars

doi:10.1016/0161-5890(83)90086-x

Cited by 5 publications

(1 citation statement)

References 37 publications

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“…In addition, it has been shown [16] that B2M polymerization is remark ably increased in patients with IgG myeloma, according to the stage of the disease. Similar findings have been reported with systemic lupus erythematosus [17], In 1983, Lôgdberg and Bjorck [18] found the binding affinity be tween B2M and serum glycoprotein of codfish and re ported the optimal conditions for binding to be at 37 °C and neutral pH. The biological significance of B2M group agglutination and the binding affinity of B2M to bacteria, methylamine, or codfish serum glycoprotein is not yet understood.…”

Section: I---------* ---------supporting

confidence: 61%

Collagen-Binding Affinity of Beta-2-Microglobulin, a Preprotein of Hemodialysis-Associated Amyloidosis

Homma¹,

Gejyo²,

Isemura³

et al. 1989

Nephron

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β₂-Microglobulin (B2M) is the amyloid preprotein that accumulates in amyloid osteoarthropathy associated with hemodialysis. To elucidate the mechanism of such amyloidogenesis, we investigated the interaction between B2M and collagen in vitro by solid-phase enzyme immunoassay. Soluble collagens which had been solidified on plastic plates were allowed to react sequentially with B2M, peroxidase-conjugated antibody to B2M, and the substrate. The collagen-binding activity was dependent on the concentration of B2M and collagen, respectively. These results suggest that the collagen-binding affinity of B2M plays an important role in amyloidogenesis.

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Section: I---------* ---------supporting

confidence: 61%