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Biomedical subjects

C W Todd

Publications and source records attributed to C W Todd.

88 records · Page 5Linked to original sources
PubMed1970

Allotype exclusion in uniform rabbit antibody to streptococcal carbohydrate.

Rabbit antibodies to streptococcal polysaccharide are described which show selectivity of expression of the allotypic specificities on both the heavy (H) and light (L) chains. One of these antibodies binds weakly to Sephadex. A purification method based on this binding has yielded antibody completely lacking any group a allotypic marker on its H chains.

Animals↗
PubMed1969

Heavy and light chain allotypic markers on rabbit homocytotropic antibody.

Evidence has been presented that rabbit homocytotropic antibody prepared against ovalbumin bears allotypic markers of both group a (heavy chain) and group b (light chain). This was shown by specific removal of activity in passive cutaneous anaphylaxis assays by anti-allotype immunoadsorbents. The homocytotropic antibody has properties which indicate that it belongs to a new class of rabbit immunoglobulin. These results demonstrate that this newly described class possesses the allotypes of both groups a and b, as has been previously shown for other rabbit immunoglobulin classes.

Adjuvants, Immunologic↗
PubMed1969

Suppression of heavy and light chain allotypic expression in homozygous rabbits through embryo transfer.

Homozygous suppression of allotypic specificities on both the heavy and light chains of rabbit immunoglobulin has been achieved by two methods involving embryo transfer. In the first method, young were transplanted into does producing antibody against an allotypic specificity homozygously present in the genome of the embryo. In this case, the suppression is caused by antibody transmitted in utero. In the second method, young from a nonimmunized surrogate mother lacking their allotypic genotype are injected neonatally with the antiallotype serum. Release from homozygous suppression appears to be achieved more readily than from heterozygous suppression.

Allergy and Immunology↗
PubMedDate not supplied

Cloning and expression in Escherichia coli of the gene for human tumour necrosis factor.

Tumour necrosis factor (TNF) was found originally in mouse serum after intravenous injection of bacterial endotoxin into mice primed with viable Mycobacterium bovis, strain Bacillus Calmette-Guerin (BCG). TNF-containing serum from mice is cytotoxic or cytostatic to a number of mouse and human transformed cell lines, but less or not toxic to normal cells in vitro. It causes necrosis of transplantable tumours in mice. TNF also occurs in serum of rat, rabbit and guinea pig. Rabbit TNF has been purified recently to give a single band on SDS-polyacrylamide gel electrophoresis (PAGE). The purified TNF had a relative molecular mass (Mr) 40,000 +/- 5,000 measured by gel filtration, and 17,000 by SDS-PAGE. Its isoelectric point is 5.0 +/- 0.3. The necrotic activity in vivo and the cytotoxicity in vitro are produced by the same substance. The gene encoding TNF has been identified in a human genomic DNA library using as a probe a cloned cDNA encoding a portion of rabbit TNF. The regions of this gene encoding an amino-acid sequence corresponding to mature TNF have been expressed in Escherichia coli and the product of this expression isolated in pure form and shown to produce necrosis of murine tumours in vivo.

Amino Acid Sequence↗