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Biomedical subjects

C Lapresle

Publications and source records attributed to C Lapresle.

59 records · Page 4Linked to original sources
PubMedDate not supplied

[Plasmodium falciparum malaria attacks with low or negative parasitemia on returning from areas of endemic resistance to 4-aminoquinolines].

Twelve recent cases of Plasmodium falciparum malaria presented with unusual clinical and laboratory features. All patients had regularly been taking adequate doses of amino-4-quinolines as prophylaxis. In most cases the symptoms were mild as compared with those in a group of 20 control patients with typical malaria. More surprisingly, parasitaemia was either negative or very weakly positive (less than 1000 infested erythrocytes per mm3). All cases occurred in people returning from areas in which resistance of P. falciparum to these drugs is endemic. Diagnostic problems could be solved in most patients by new immunological techniques relying on the detection of parasitized erythrocytes and plasmodium antigens using a battery of monoclonal antibodies. A physiopathological model explaining why parasitaemia is negative in such cases is suggested.

Amodiaquine↗
PubMedDate not supplied

Enzyme-linked immunosorbent assay for measurement of penicilloyl groups.

An enzyme-linked immunosorbent assay for measuring penicillin groups is described. Alkaline phosphatase conjugated to penicilloyl residue was reacted with purified anti-penicilloyl antibodies coated upon polystyrene plates. The inhibition of this reaction allowed a specific determination of penicilloyl residues at the picomole level. This assay was applied to the study of the penicilloyl groups linked to human albumin and to the measurement of some of these groups after enzymatic degradation or physical modifications of the albumin molecule.

Alkaline Phosphatase↗
PubMedDate not supplied

[Immunochemical properties of cyanogen bromide fragments of human serum albumin (author's transl)].

Fragments A, B and C obtained by CNBr degradation of human serum albumin (HSA) were studied by specific quantitative precipitation with anti-HSA sera. A co-precipitation has been observed between fragments B and C as well as between C and A which follow each others in the albumin molecule. On the contrary, there was no co-precipitation between fragments B and A which correspond respectively to the N- and C-terminal part of the albumin molecule. Moreover, using inhibition of passive haemagglutination, it has been observed that fragment A does not inhibit anti-B antibodies and fragment B does not inhibit anti-A antibodies. These results indicate that there are common antigenic sites to fragments B and C as well as to C and A but not to B and A. This is in agreement with the data upon the structure of HSA showing that it is made of three domains in linear sequence.

Animals↗