Binding of lysozyme to brush border membranes of rat kidney |
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Authors: | Gabriele Beyer Folkert Bode Karl Baumann |
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Affiliation: | Department of Cell Physiology, Institute of Physiology, University of Hamburg, Grindelallee 117, 2000 Hamburg 13 F.R.G. |
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Abstract: | 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 μM 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. |
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Keywords: | Lysozyme Enzyme-membrane interaction Protein reabsorption Endocytosis Amino acid effect (Rat kidney cortex) |
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