Binding of lysozyme to brush border membranes of rat kidney.
The binding of 125I-labelled egg-white lysozyme to isolated brush border membranes of rat kidney cortex was investigated. The lysozyme binding was reversible and saturable. The Scatchard plot revealed a one-component binding type with a dissociation constant of 7.8 microM and 15.6 nmol/mg membrane protein for the number of binding sites. The binding of the basic lysozyme could be reduced by basic amino acids such as L-lysine, L-ornithine or L-arginine, while neutral amino acids such as L-citrulline or L-alanine had no effect. The inhibitory effect of lysine was competitive.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002645:Chickens; D004529:Egg White; D007457:Iodine Radioisotopes; D007672:Kidney Cortex / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008871:Microvilli / Q000378:metabolism*; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains
D007457:Iodine Radioisotopes; D009113:Muramidase