title: Protein-membrane interactions: equilibrium adsorption and binding of proteins and polyamino acids on erythroblasts transformed by Friend virus.
abstract: 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.
mesh_terms: 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
chemical_list: D010455:Peptides; D011506:Proteins; D005780:Gelatin; D010047:Ovalbumin; D009113:Muramidase