Biomedical subjects
Publications and source records attributed to F Guilleux.
Studies of human breast cancers show that tumoral tissues have a much higher ferritin content (mean : 4,5 times) than normal tissues. However, only 10% of patients without metastasis present raised levels of serum ferritin, whereas hyperferritinemia is observed in almost 95% of patients with liver, bone or lung metastasis.
Membrane-bound phosphorylatable proteolipids were reported to play a role in the regulation of transmembrane Ca2+ fluxes by catecholamines. A generally applicable purification procedure is described by which such proteolipids as the cardiac sarcoplasmic reticulum phospholamban is purified by solvent extraction followed by high pressure liquid chromatography on microparticulate silica. Phospholamban is thereby purified with a yield of 3.37 mg from 100 mg of sarcoplasmic reticulum proteins, significantly higher than that obtained by any of the previously reported procedures. It appeared homogeneous upon dodecyl sulfate-polyacrylamide gel electrophoresis where it is stained by Coomassie blue and detected by autoradiography. The same procedure is applicable to cardiac sarcolemmal calciductin. Both proteolipids exhibit the same Mr 11 000 and pI 3.7 upon two-dimensional gel electrophoresis. Their amino acid compositions are very similar if not identical. This raises the intriguing possibility that phospholamban and calciductin are identical though they obviously belong to different membranes.
Ferritin, iron storage protein, presents two types of subunits, H and L, the respective proportions of which varying with the tissue of origin and defining molecules called isoferritins. This work attempts to compare four human ferritins (from liver, spleen, heart and placenta) by means of the microcomplement fixation technique. Results show that placenta and liver ferritins are closely related, while slight but significant differences appear between liver, spleen and heart ferritins. These differences are obviously less important compared to those observed between ferritins from different species of origin, as shown by the results expressed in terms of index of dissimilarity or immunological distance. Those results are fully consistent with the elementary aminoacid composition as well as with the relative proportions of H and L subunits among the various types of human isoferritins we have studied.
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A variant of a partially purified Placental Alkaline Phosphatase, showing a slow electrophoretic mobility but the same kinetic caracteristics as the common type, has been found. This variant also differs from the D type by its insensibility to L-leucine inhibition.
Polyacrylamide gradient gel electrophoresis may be used to separate placental alkaline phosphatase from other types of serum alkaline phosphatase. This method, of which specificity is demonstrated by the thermostability and immunological reaction of the placental form, is sensitive enough to detect an activity of 0.02 mU in a sample, and seems suitable for use in investigating placental isoenzyme in serum.
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Explore the source record for details and available documents.
Explore the source record for details and available documents.