[Isolation and partial study of an anti-hemoglobine precipitine in "Biomphalaria glabrata" (author's transl)].
A protein (PaHb) with a precipiting capacity with regard to normal and pathological human hemoglobin as well as horse and hen hemoglobin has been separated on immunoadsorbent from hemolymph of Biomphalaria glabrata. The joining of PaHb and hemoglobin takes place at the level of the polypeptidic chain. A reconnaissance of the spatial structure of the globin seems to exist. The absence of heme does not lead to a decrease in the intensity of the reaction. The coefficient of the sedimentation of PaHb is of 2.74 S and its molecular weight has been estimated at 47,000 per chromatography in thin layer. The divalent cation MgCl2 strengthens the intensity of the reaction, as for CaCl2 no change is observed, and in the presence of sodium citrate one observes a clear decrease in the reaction. The intensifying of the reaction when in presence of divalent cation MgCl2 could be the result of a stabilization or an activation of the natural structure of PaHb when in presence of Mg. PaHb shows no fonctional impairment after exposure at 65 degrees C during 45 min. The localization of PaHb in the total antigenic structure of the hemolymph is situated around the level of the 5th precipitine line. The functional role of the protein seems to carry the hemoprotein of the hemolymph.
D000818:Animals; D001700:Biomphalaria / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D002413:Cations, Divalent; D002645:Chickens; D006454:Hemoglobins / Q000378:metabolism*; D006458:Hemolymph / Q000378:metabolism; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D011234:Precipitins / Q000032:analysis / Q000096:biosynthesis*
D002413:Cations, Divalent; D006454:Hemoglobins; D011234:Precipitins; D008274:Magnesium; D002118:Calcium
Isolement et étude partielle d'une précipitine anti-hémoglobine chez Biomphalaria glabrata