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Biomedical subjects

R P Triglia

Publications and source records attributed to R P Triglia.

5 recordsLinked to original sources
PubMed1981

The bovine complement system.

Methods were developed for titrating bovine C3b-inactivator, C2, C3 and C4 by non-hemolytic means, and for assaying by hemolysis all the components of the bovine classical complement system except C2. All components were detected at serum dilutions above 1:1000, and some at dilutions above 1:100,000. C1, C4, C5, C7 and C9 titers were very high in adult bovine serum, and C2 and C8 were relatively low. C1, C2, and C8 were quite heat-labile at 56 degrees C, and C7 was moderately so, while C3 amd C6 titers increased after heating due to inactivation of a heat-labile inhibitor. Fetal bovine serum contained approximately 1-3% of adult levels of conglutinin, C1 and C6, and 5-50% of adult levels of the remaining components except C3. C3 antigen was found, but C3 functional activity was undetectable in most fetal bovine sera, though present at low levels in a few.

Animals↗
PubMed1978

Evidence that bovine conglutinin reacts with an early product of C3b degradation, and an improved conglutination assay.

When EAC43b were treated with heated serum in EDTA, reactivity with bovine conglutinin appeared rapidly, even at 0 degrees C, and almost simultaneously with the loss of C3b rosetting capacity. At the time conglutinability first appeared, there was no detectable decrease in I-A or hemolytic C3 activity, and no detectable C3 antigen release from the cells. With prolonged exposure to heated serum in EDTA, I-A (immune adherence) and hemolytic C3 activity were lost. If this exposure was at 37 degrees C, C3 antigen became strongly detectable in the supernatant fluid, and eventually conglutinability was markedly reduced or lost, whereas C3d rosettes were unaffected. We suggest that bovine conglutinin reacts with some early product of C3b degradation, rather than with C3d, and propose that this intermediate be designated C3k. We have developed a semi-quantitative assay for bovine conglutinin, utilizing a Coulter Counter to register the decrease in total particles due to red cell aggregation. By using this method, we have detected conglutination with mouse complement (C) as well as with that from man and the guinea pig.

Animals↗
PubMed1977

Improved efficiency of mouse, guinea pig and human C3b inactivator at low ionic strength, and reproducible immune-adherence with mouse complement.

Inactivation of homologous C3b by heated guinea pig, mouse and human serum was found to be much more rapid and complete at low ionic strength (0.037) than at micron = 0.15. The C3b inactivator in human and mouse serum was somewhat unstable to heating at 56 degrees C. Heated guinea pig serum showed the greatest ability to inactivate heterologous C3b, and human serum the least. Suramin (1 mg/ml) completely blocked homologous C3b inactivation by heated human, guinea pig and mouse serum, and 0.1 mg/ml was effective with mouse but not with human or guinea pig serum. Immune-adherence reactions with mouse C3 produced somewhat unstable hemagglutination patterns, which were improved by using ovalbumin in the buffer and minimizing EAC exposure to warm temperatures. A prozone phenomenon was frequently observed in immune-adherence hemagglutination with mouse C3, and less frequently with guinea pig and human C3.

Animals↗