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Biomedical subjects

L E CLUFF

Publications and source records attributed to L E CLUFF.

At least 55 records · Page 3Linked to original sources
PubMed1956

A study of the effect of serum on the immunological reaction of a bacterial endotoxin.

Contact of a purified endotoxin from Shigella fiexneri Type Z with normal rabbit or human serum results in an alteration of its immunological reaction with antiserum, as determined by precipitation in gel. Analysis of fractions of normal serum obtained by zone electrophoresis in starch indicates that the component responsible for altering the immunological reaction of endotoxin is associated with beta globulin. Normal serum has no similar effect on the immunological reaction of a variety of other protein and polysaccharide antigens. Serum from rabbits made tolerant to the pyrogenic action of an endotoxin from Serratia marcescens (P-35) possesses the ability to alter the reaction of Shigella endotoxin with its specific antiserum, although the serum from tolerant rabbits does not significantly enhance the pyrogenicity of Shigella toxm. The component of normal rabbit serum responsible for the effect on the immunological reaction of Shigella endotoxin is not destroyed by heating at 56 degrees C. The possible relationship of the effect of normal serum on the immunological reaction of endotoxin and the augmentation of fever induced by endotoxins is discussed.

Animals↗
PubMed1954

Immunochemical study of a bacterial endotoxin: Shigella flexneri type Z.

The endotoxins of the Gram-negative bacteria have similar biological and chemical properties. The toxic antigen of Shigella flexneri Type Z was selected as a representative endotoxin, and it was confirmed that the antigen consists of a polysaccharide conjugated with phospholipid and protein. By the technique of zone electrophoresis, the polysaccharide of the purified endotoxin was shown to be conjugated with each of three different proteins, and each conjugate proved toxic and antigenic for the rabbit. Two of the protein conjugates were digested by trypsin and the released polysaccharide appeared to conjugate with the remaining trypsin-resistant protein. Immunological analysis revealed that the purified toxic antigen is heterogeneous and that the polysaccharide and protein components possessed serological activity. The trypsin-treated toxin had a single electrophoretic zone and its precipitation in gel suggested immunological purity. Proteolytic treatment of the endotoxin did not destroy its toxicity or antigenicity for the rabbit.

Animals↗