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Purification, cloning and nucleotide sequence determination of cynomolgus monkey apolipoprotein C-11: comparison to the human sequence

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Abstract

We have purified apolipoprotein C-II (apo C-II) from cynomolgus monkey plasma, prepared antibody against it and used the antibody to isolate a cDNA containing the complete coding sequence for cynomolgus monkey apo C-11. Sequence analysis indicated that the monkey apo C-11 cDNA was 200 by longer than the human and the difference in size was all in the 5° untranslated region of the mRNA. This was confirmed by Northern analysis of human and monkey RNA. There was an open reading frame in the monkey apo C-11 cDNA sequence encoding a preprotein of 101 amino acids — identical in size to the human protein. The carboxyl terminal 44 amino acids of the protein were 100% homologous to the human apo C-11 amino acid sequence indicating evolutionary conservation of both structure and function. However, the amino terminal 35 amino acids of the protein were only 75% homologous and the amino terminal 19 amino acids were only 58% homologous to the human sequence. The amino acid sequence derived from the nucleotide sequence predicts a more basic protein than the human apo C-11 and this is confirmed by isoelectric focusing and immunoblotting.

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Authors and Affiliations

  1. Molecular Biology Research, The Upjohn Company, 301 Henrietta Street, 49007, Kalamazoo, MI, USA

    B. E. Whitted, H. G. Polites & K. R. Marotti

  2. Metabolic Diseases Research, The Upjohn Company, 301 Henrietta Street, 49007, Kalamazoo, MI, USA

    C. K. Castle & G. W. Melchior

Authors
  1. B. E. Whitted
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  2. C. K. Castle
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  3. H. G. Polites
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  4. G. W. Melchior
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  5. K. R. Marotti
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Whitted, B.E., Castle, C.K., Polites, H.G. et al. Purification, cloning and nucleotide sequence determination of cynomolgus monkey apolipoprotein C-11: comparison to the human sequence. Mol Cell Biochem 90, 69–79 (1989). https://doi.org/10.1007/BF00225222

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  • DOI: https://doi.org/10.1007/BF00225222

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