Protein-membrane interactions: equilibrium adsorption and binding of proteins and polyamino acids on erythroblasts transformed by Friend virus.
Equilibrium adsorption and binding isotherms at different pH values and temperatures were used to study the mechanism of interaction of 6 proteinaceous compounds with erythroblasts transformed by Friend virus (HFL cells). The molecular weight of the adsorbate appeared to influence the amounts absorbed: fewer moles interacted with increasing molecular weight. The pI value affected binding of adsorbates of low molecular weight in an almost linear way: more moles bound with increasing pI value. Polylysine and polysarcosine absorbed to labile components on the cell surface. Gelatin, lysozyme, ovalbumin, and polysarcosine interacted with pronase-susceptible, Concanavalin A and polylysine with non-susceptible components.
D000327:Adsorption; D000818:Animals; D002460:Cell Line; D002472:Cell Transformation, Viral; D004900:Erythroblasts / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005622:Friend murine leukemia virus; D005780:Gelatin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D051379:Mice; D008970:Molecular Weight; D009113:Muramidase / Q000378:metabolism; D010047:Ovalbumin / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D013696:Temperature
D010455:Peptides; D011506:Proteins; D005780:Gelatin; D010047:Ovalbumin; D009113:Muramidase