Surface hydrophobicity of proteins and selectivity of intracellular proteolysis.
The affinity of cytosol proteins from protein-free fed rats to hydrophobic surfaces is diminished in comparison to the affinity of cytosol proteins from normal or protein-rich fed rats. Furthermore, the affinity of these cytosol proteins to hydrophobic surfaces in the presence of ultrafiltrates from cytosol of rats fed previously a protein-rich diet or a protein-free diet is diminished. Ultrafiltration itself increases the affinity of cytosol proteins to hydrophobic surfaces (octyl-sepharose or phenyl-sepharose).
D000818:Animals; D003600:Cytosol / Q000378:metabolism*; D004044:Dietary Proteins / Q000008:administration & dosage*; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D012685:Sepharose / Q000031:analogs & derivatives; D013499:Surface Properties; D014462:Ultrafiltration
D004044:Dietary Proteins; D011506:Proteins; C027176:octyl-sepharose CL-4B; C020927:phenyl-sepharose; D012685:Sepharose; D010447:Peptide Hydrolases