Screening of antiaggregating and antithrombotic agents using a quantitative in vivo model.
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Biomedical subjects
Publications and source records attributed to R Bourgain.
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The observations of surface electromaps recorded at rest and during exercise in two examplative cases are reported: the first one deals with a normal man while the second refers to a patient suffering from an old inferior myocardial infarction with bouts of angina pectoris; these surface maps are compared with myocardial scanning also performed at rest and during exercise. Special attention is devoted to the possible relation of the above described, non-invasive, techniques to the anatomical description of coronary lesions as demonstrated by coronary angiography. A close relationship is found between the surface potential distribution pattern and the area of hypofixation observed on the scan as far as the presumed location of ischemic myocardial tissue is concerned.
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In this report the structure of the novel polypeptide h3, isolated from subsets of tissues of a single species, and the structural similarity between interspecies h3 were investigated by peptide mapping of enzymatic and chemical cleavage fragments of h3 in one-dimensional SDS-PAGE; the peptide maps were commented on in comparison with the known sequence of 21 kDa protein, a h3-like ox brain protein. The following results were obtained: peptides generated by chymotrypsin, protease XX, BNPS-skatole and CNBr cleavage of different tissues in a single species were strikingly identical, whereas peptide maps obtained from analogue tissues in different species revealed slight structural differences. Possible ligand-h3 binding was studied by comparing the c.d. spectra of native h3, and h3 incubated with several phospholipids. Given the presence of h3 or h3-like protein in rat and human platelets, h3 was also assessed in platelet aggregation in the presence of h3 and specific anti-h3 antiserum. So far, the results emphasize the unique intra- and interspecies molecular form of h3, allow us to assign to known amino acid sequence of 21 kDa to a large extent to human h3, but do not identify h3 as a phospholipid binding protein.