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  • Title: Bindings of plasma proteins to streptococci of serological group L with special reference to their immunoglobulin G Fc-receptor activity.
    Author: Lämmler C, Schaufuss P, Frede C, Blobel H.
    Journal: Can J Microbiol; 1988 Jan; 34(1):1-5. PubMed ID: 2454150.
    Abstract:
    Of 33 streptococcal cultures belonging to serological group L, all bound human immunoglobulin (Ig) G, fibrinogen, and fibronectin; 32 bound bovine IgG; 31 bound alpha 2-macroglobulin; 5 bound albumin; and none bound either haptoglobin or IgA. The binding sites for IgG could be isolated from the L streptococci by trypsinization and purified by affinity chromatography on human IgG-Sepharose. The purified Fc receptors reacted with IgG subclasses 1, 2, 3, 4 of humans, 1 and 2 of bovines, ovines, and caprines as well as a, b, c, and T of equines. They had a molecular mass of approximately 49,000 Da. Thus, the Fc receptors from L streptococci corresponded to type III Fc receptors of Streptococcus dysgalactiae.
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