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Immunoglobulin abnormalities in families of patients with Waldenström's macroglobulinemia.
Abstract Immunologic studies were performed on the serums of 216 relatives of sixty-five patients with Waldenstrom's macroglobulinemia. Three kinds of abnormalities were found: (1) AnExpand
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Immunochemical studies in four cases of alpha chain disease.
Studies of a number of properties of the pathological gammaA-proteins in the first four cases of the recently recognized alpha-chain disease demonstrate that, as in gamma-heavy-chain disease, theExpand
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Characterization of jacalin, the human IgA and IgD binding lectin from jackfruit.
The lectin jacalin from the jackfruit Artocarpus heterophyllus reacts by precipitation and western blotting with human IgA1 and IgD but not with IgA2 (nor IgG and IgM). However, it weakly binds IgA2Expand
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[Structure of the immunoglobulins].
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MU-chain disease in an African patient.
A new case of µ-chain disease occurring in an African patient is described. The main clinical feature was a massive splenomegaly. Contrary to five previously reported cases, this patient was notExpand
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Physicochemical and immunological properties of a mu chain disease protein.
Abstract The physicochemical and immunological properties of a μ heavy chain disease protein (BO) have been investigated. The native protein has a mol. wt of 520,000 daltons and it is constituted ofExpand
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Variable J‐chain content in human IgM
Human IgM consists of 10 heavy '/a' chains and 10 light-chains interlinked by disulfide bridges and organized in 5 subunits (IgM's) each containing 2 '/l'and 2 light-chains. An additional polypeptideExpand
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Binding of human hemoglobin and its polypeptide chains with haptoglobin coupled to an agarose matrix.
The interactions of human haptoglobin covalently linked to agarose with human hemoglobin and with p-chloromercuribenzoic-acid-treated alpha and beta chains (alpha* and beta* chains) were studied byExpand
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The inter‐chain disulfide bonds of a μ‐chain disease protein
Heavy chain disease proteins are homogeneous lg molecules lacking the light polypeptide chains and composed of incomplete heavy chains, present in the serum of patients with lymphoproliferativeExpand
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Affinity chromatography: specific binding of hemoglobin on agarose linked haptoglobin.
Abstract Human haptoglobin was coupled to agarose and used as affinity adsorbant to bind human hemoglobin. The optimal conditions of hemoglobin binding and dissociation were defined. It was foundExpand
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