Interaction of polylysine with soluble components of human erythrocyte membranes

Abstract

• 1.

  1. The interactions of poly-l-lysine with soluble erythrocyte components and with Collocalia mucoid, a sialoprotein of avian origin, were studied by electrophoresis and immuno-electrophoresis in agar gel.

• 2.

  2. Polylysine combined with erythrocyte membrane glycoprotein and with Collocalia mucoid to form visible precipitates in agar gel; erythrocyte fractions devoid of glycoprotein failed so to react.

• 3.

  3. A precipitate of virus receptor substance with polylysine could be quantitatively redissolved by the addition of poly-l-aspartic acid to the mixture. Whether this change in solubility occurred as a result of displacement of polylysine from the glycoprotein or by the formation of soluble complexes could not be established.

• 4.

  4. Neuraminidase (EC 3.2.1.18) treatment of erythrocyte glycoproteins and Collocalia mucoid greatly reduced or abolished their capacity to precipitate with polylysine.

• 5.

  5. The findings suggest that N-acetylneuraminic acid in the acid glycoprotein of erythrocyte membranes is an important factor in the agglutination of erythrocytes by polybases, a phenomenon thought to have some bearing on intravascular thrombus formation.