Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16).

Yamamoto, K; Sugita, N; Kobayashi, T; Okuda, K; Van De Winkel, J G; Yoshie, H

Yamamoto, K; Sugita, N; Kobayashi, T; Okuda, K; Van De Winkel, J G; Yoshie, H.

Affiliation

Yamamoto K; Department of Periodontology, Faculty of Dentistry, Niigata University, Niigata, Japan.

Tissue Antigens ; 57(4): 363-6, 2001 Apr.

Article in En | MEDLINE | ID: mdl-11380948

Subject(s)

Polymorphism, Genetic/immunology; Receptors, IgG/genetics; Receptors, IgG/metabolism; Amino Acid Sequence; Amino Acid Substitution/genetics; Base Sequence; Carbohydrate Conformation; Female; Glycosylation; Heterozygote; Humans; Ligands; Male; Molecular Sequence Data; Neutrophils/immunology; Phagocytosis/genetics; Receptors, IgG/isolation & purification

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Collection: 01-internacional Database: MEDLINE Main subject: Polymorphism, Genetic / Receptors, IgG Limits: Female / Humans / Male Language: En Journal: Tissue Antigens Year: 2001 Document type: Article Affiliation country: Japan Country of publication: United kingdom

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