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Amino terminal sequence of heavy and light chains from ratfish immunoglobulin

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Abstract

The ratfish,Callorhinchus callorhinchus, a representative of the Holocephali, has a natural serum hemagglutinin (M r 960 000), composed of heavy (M r 71000), light (M r 22 500), and J (M r 16 000) chains. To approach the mechanisms that generate diversity at this level of evolution, the amino terminal sequence of the heavy and light chains was determined by automated microsequencing. The chains are unblocked and have modest internal sequence heterogeneity. The heavy chains show sequence similarity with the terminal region of the heavy chain from the horned shark,Heterodontus francisci, and other species. In contrast to the heavy chain, the ratfish light chains display low sequence similarity with their shark kappa counterparts. However, their similarity with the variable region of the chicken lambda light chains is about 75%.

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Author notes

  1. Héctor L. Aguila

    Present address: Department of Pathology S205, Stanford University, School of Medicine, Stanford University Medical Center, 94305-5324, Stanford, CA, USA

Authors and Affiliations

  1. Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Casilla 114-D, Santiago, Chile

    Alfredo E. De Ioannes & Héctor L. Aguila

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  1. Alfredo E. De Ioannes
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  2. Héctor L. Aguila
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De Ioannes, A.E., Aguila, H.L. Amino terminal sequence of heavy and light chains from ratfish immunoglobulin. Immunogenetics 30, 175–180 (1989). https://doi.org/10.1007/BF02421203

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  • DOI: https://doi.org/10.1007/BF02421203

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