Literature DB >> 7213352

Thermodynamic studies on the hydrolysis of cytidine 2':3'-phosphate by bovine pancreatic ribonuclease A. A possible effect of the change of the structure of water.

J A Biosca, C M Cuchillo.   

Abstract

The temperature-dependence of the ribonuclease A-catalysed hydrolysis of cytidine 2':3'-phosphate was studied in the range of temperatures 0--40 degrees C. A break at 4 degrees C was found both in the Arrhenius and the van't Hoff plots. It is likely that the transition observed is due to the change in the structure of water.

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Year:  1980        PMID: 7213352      PMCID: PMC1162049          DOI: 10.1042/bj1890655

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  5 in total

1.  Chromatography of ribonuclease on carboxymethyl cellulose columns.

Authors:  G TABORSKY
Journal:  J Biol Chem       Date:  1959-10       Impact factor: 5.157

2.  Some spectrophotometric and polarimetric experiments with ribonuclease.

Authors:  M SELA; C B ANFINSEN
Journal:  Biochim Biophys Acta       Date:  1957-05

3.  The active site and mechanism of action of bovine pancreatic ribonuclease. 7. The catalytic mechanism.

Authors:  D Findlay; D G Herries; A P Mathias; B R Rabin; C A Ross
Journal:  Biochem J       Date:  1962-10       Impact factor: 3.857

4.  Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease.

Authors:  G G Hammes; P R Schimmel
Journal:  J Am Chem Soc       Date:  1965-11-05       Impact factor: 15.419

5.  Steady-state kinetic study of action of ribonuclease A, involving a conformational change between 30 and 40 degrees C.

Authors:  R R Matheson; H A Scheraga
Journal:  Biochemistry       Date:  1979-06-12       Impact factor: 3.162

  5 in total

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