1. 1. The binding of 5'AMP, 5'GMP, 5'CMP, 3/CMP and Cl6RMP to RNAase A was studied by means of the gel filtration technique. 2. 2. It was found that only one molecule of 3'CMP binds strongly to the enzyme although a very unspecific binding is also present. 3. 3. The interaction of 5'AMP and 5'GMP with the enzyme shows one strong binding site and several weak binding sites, whereas two molecules of 5'CMP bind to RNAase A with equal strength. Cl'RMP shows an anomalous behaviour as both split peaks and troughs are found in the chromatogram. 4. 4. The Ka, values for 3'CMP and the strong binding site of 5'AMP and 5'GMP are very similar whereas that for the two binding sites of 5'CMP is smaller (about 2.2 × 10-4M-1 and 0.5 × 10-4M-1, respectively at pH 5.5, I = 0.01 and 25°C). 5. 5. The results are in general agreement with the known multiplicity of ligand-binding subsites in RNAase A. © 1984.
|Journal||International Journal of Biochemistry|
|Publication status||Published - 1 Jan 1984|