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Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
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Published on: December 15, 2011

An abnormal human IgA1 half-molecule

Y S Kang, B S Shim

    Biochimica Et Biophysica Acta
    |October 26, 1977
    PubMed

    An IgA1 half-molecule, which is composed of a deleted alpha1 chain linked with a disulfide bond to an intact kappa chain, was detected in a patient (Cha). The molecular weights of the paraprotein and the isolated alpha1 chain were estimated to be 75 000 and 53 000, respectively. Identification of tyrosine as the C-terminal amino acid and the presence of idiotypic determinants in the abnormal alpha1 chain indicated that the molecule would have an intact N-terminal variable region and a C-terminal region. Furthermore, no cleavage of the abnormal protein into Fab and Fc by proteolytic enzyme isolated from Neisseria gonorrhoeae suggested the absence of a "hinge" region in the abnormal alpha1 chain.

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