The properties of the interaction between bovine pancreatic ribonuclease A and mononucleotides supports the existence of several binding sub-sites in the enzyme

Alícia Guasch; Joan Sola; M. Victòria Nogués; Xavier Parés; Claudi M. Cuchillo

doi:https://doi.org/10.1016/0020-711X(84)90090-9

The properties of the interaction between bovine pancreatic ribonuclease A and mononucleotides supports the existence of several binding sub-sites in the enzyme

Alícia Guasch, Joan Sola, M. Victòria Nogués, Xavier Parés, Claudi M. Cuchillo

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

5 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1071-1075
Journal	International Journal of Biochemistry
Volume	16
DOIs	https://doi.org/10.1016/0020-711X(84)90090-9
Publication status	Published - 1 Jan 1984

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@article{1f90b8d83d4341a2ac5e9b1cbe09b4cb,

title = "The properties of the interaction between bovine pancreatic ribonuclease A and mononucleotides supports the existence of several binding sub-sites in the enzyme",

abstract = "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. {\textcopyright} 1984.",

author = "Al{\'i}cia Guasch and Joan Sola and Nogu{\'e}s, {M. Vict{\`o}ria} and Xavier Par{\'e}s and Cuchillo, {Claudi M.}",

year = "1984",

month = jan,

day = "1",

doi = "https://doi.org/10.1016/0020-711X(84)90090-9",

language = "English",

volume = "16",

pages = "1071--1075",

}

The properties of the interaction between bovine pancreatic ribonuclease A and mononucleotides supports the existence of several binding sub-sites in the enzyme. / Guasch, Alícia; Sola, Joan; Nogués, M. Victòria; Parés, Xavier; Cuchillo, Claudi M.

In: International Journal of Biochemistry, Vol. 16, 01.01.1984, p. 1071-1075.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - The properties of the interaction between bovine pancreatic ribonuclease A and mononucleotides supports the existence of several binding sub-sites in the enzyme

AU - Guasch, Alícia

AU - Sola, Joan

AU - Nogués, M. Victòria

AU - Parés, Xavier

AU - Cuchillo, Claudi M.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - 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.

AB - 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.

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DO - https://doi.org/10.1016/0020-711X(84)90090-9

M3 - Article

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EP - 1075

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