Letter | Published:

Further Evidence for Macromolecular Nature of Human C′l

Naturevolume 214pages185186 (1967) | Download Citation

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Abstract

C′l activity of human complement has been shown by Lepow et al.1 to require three chromatographically isolated proteins: C′lq, C′lr and C′ls. The C′lq component was identical to the 11S protein, originally described by Müller-Eberhard and Kunkel2 and Taranta et al.3. C′lr was a previously undescribed protein and C′ls the known pro-esterase. Further experiments demonstrated that these sub-components formed a macromolecule in the presence of calcium with a sedimentation coefficient of 18, whereas in sodium ethylenamine tetraacetate (NaEDTA), C′l dissociated into its three sub-components, C′lq, C′lr and C′ls (ref. 4), with sedimentation coefficients of 11S, 7S and 4S, respectively. The macromolecular nature of C′l was obtained by haemolytic data alone, and so the following experiments were designed to demonstrate these differences in sedimentation utilizing an antiserum specific for the 11S protein or C′lq.

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References

  1. 1

    Lepow, I. H., Naff, G. B., Todd, E. W., Pensky, J., and Hinz, jun., C. F., J. Exp. Med., 117, 983 (1963).

  2. 2

    Müller-Eberhard, H. J., and Kunkel, H. G., Proc. Soc. Exp. Biol. and Med., 106, 291 (1961).

  3. 3

    Taranta, A., Weiss, H. S., and Franklin, E. C., Nature, 189, 239 (1961).

  4. 4

    Naff, G. B., Pensky, J., and Lepow, I. H., J. Exp. Med., 119, 593 (1964).

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    Morse, J. H., and Christian, C. L., J. Exp. Med., 119, 95 (1964).

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    Hanauer, L. B., and Christian, C. L., Amer. J. Med. (in the press).

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    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., J. Biol. Chem., 193, 265 (1951).

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    Becker, E. L., J. Immunol., 84, 299 (1960).

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Affiliations

  1. Department of Medicine, Columbia University College of Physicians and Surgeons, New York

    • JANE H. MORSE

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https://doi.org/10.1038/214185a0

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