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    FEBS Lett. 1990 Aug 20;269(1):19-22.

    Neutron scattering study of the (gamma-B) catalytic domains of complement proteases activated C1r and C1s.

    Zaccaï G, Aude CA, Thielens NM, Arlaud GJ.

    Source

    CNRS URA 1333, Institut Laue Langevin, Grenoble, France.

    Abstract

    The catalytic domains of activated C1r and C1s, comprising the C-terminal region of the A chain (gamma), disulphide-linked to the B chain, were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin, respectively, and studied by small angle neutron scattering. For activated C1s (gamma-B), a molar mass of 45,000 +/- 5000 g/mol, and a relatively large radius of gyration (Rg) of 28 +/- 1 A were determined, excluding a single globular domain. The corresponding values for activated C1r (gamma-B)2 (90,000 g/mol, Rg = 34 +/- 1 A) are consistent with a dimer involving the loose packing of two (gamma-B) subunits. Various models of the dimer are discussed in the light of neutron scattering and other data.

    PMID:
    2143735
    [PubMed - indexed for MEDLINE]

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