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K Yonemasu

Publications and source records attributed to K Yonemasu.

66 records · Page 4Linked to original sources

Anti-human C1q: rapid and simple method for preparing monospecific antisera.

A new simple, rapid and economical method is described for producing monospecific antisera to human C1q without using gel filtration or column chromatography. Moderately purified C1q is obtained by dialyzing fresh human serum in the presence of chelating agents at low ionic strength and then electrophoresing it in agarose. When injected into rabbits, the electrophoretically purified product induced potent antisera to three or four serum proteins including C1q, all with slow electrophoretic mobilities (gamma to beta) at pH 8.6. The antibodies to serum proteins other than C1q are easily removed by immunoadsorbents consisting of the insolubilized supernatants obtained from the dialysis used to make the original C1q-rich fraction. The monospecific antisera prepared by this technique form only one band of precipitate in the slow gamma region in immunoelectrophoresis with whole human serum or C1q-rich solution, as well as in Ouchterlony double diffusion test. They agglutinate EAClq but not EA cells and detect the same antigen as standard monospecific antisera to human C1q obtained by another well-established method.

Adsorption↗

Ultrastructure of the human complement component, Clq (negative staining-glutamine synthetase-biologically active Clq).

The human complement component, Clq, is a fragile molecule of delicate structure consisting of three distinct parts, a central subunit, connecting strands, and terminal subunits. Each terminal subunit is further subdivided into a large and a small subunit, and the central subunit appears to be divided into two equal parts. In the intact molecule, six connecting strands link six terminal subunits by their larger subdivision to the central subunit. The overall diameter of the molecule when viewed from the "top" is about 35 nm (350 A).

Centrifugation↗

Antigenic determinants resulting from polymerization of immunoglobulin G.

Antibodies against heat-aggregated human IgG (AHG) were raised in rabbits and those against immune complex (IC) of tetanus toxoid and its human antitoxin (T/aT) in rabbits and mice. These antisera were analyzed by the Ouchterlony double diffusion technique against native monomeric human IgG (NHG), AHG and chemically linked human IgG (poly-G). The appearance of neoantigens was demonstrated with human IgG bound to its corresponding antigen or denaturated nonspecifically. The results are indicative of the existence of a common determinant shared with AHG and T/aT, in addition to those of their own.

Animals↗