1. The subunit structure of rabbit subcomponent C1q was examined in a previous publication (Reid et al., 1972). The present paper describes some aspects of the structure of the polypeptide chains derived from the molecule. 2. The three polypeptide chains, produced by performic oxidation, of rabbit subcomponent C1q were isolated by ion-exchange chromatography in 8m-urea on DEAE-cellulose. 3. Each chain was found to contain 15–18% glycine and significant amounts of the amino acids hydroxyproline and hydroxylysine. 4. By means of collagenase digestion it was shown that all three chains of rabbit subcomponent C1q contain collagen-like sequences of amino acids which constitute about 40% of each chain. 5. By use of carboxypeptidase A it was established, indirectly, that the collagen-like sequences, in one of the chains, are probably located near, or at, the N-terminal end of the chain. 6. Collagenase digestion and heating at 52°C (but not at 49°C) caused rapid loss of native rabbit subcomponent C1q haemolytic activity.
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November 1974
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Research Article|
November 01 1974
Studies on the structure and activity of rabbit C1q (a subcomponent of the first component of complement)
Diane M. Lowe;
Diane M. Lowe
1Medical Research Council Immunochemistry Unit, Department of Biochemistry. University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
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Kenneth B. M. Reid
Kenneth B. M. Reid
1Medical Research Council Immunochemistry Unit, Department of Biochemistry. University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1974 London: The Biochemical Society
1974
Biochem J (1974) 143 (2): 265–272.
Citation
Diane M. Lowe, Kenneth B. M. Reid; Studies on the structure and activity of rabbit C1q (a subcomponent of the first component of complement). Biochem J 1 November 1974; 143 (2): 265–272. doi: https://doi.org/10.1042/bj1430265
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