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Co-operativity in seminal ribonuclease function: binding studies.

A Di Donato, R Piccoli, G D'Alessio

    The Biochemical Journal
    |January 15, 1987
    PubMed
    Summary
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    Bovine seminal RNAase exhibits unique nucleotide binding, showing distinct site discrimination and mixed cooperativity. This clarifies enzyme kinetics, ruling out hysteretic effects.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Bovine seminal RNAase (BS-RNAase) is an enzyme with two active sites.
    • Understanding nucleotide binding is crucial for enzyme kinetics.

    Purpose of the Study:

    • To investigate nucleotide binding to BS-RNAase.
    • To elucidate the kinetics of the hydrolytic step.

    Main Methods:

    • Differential spectrophotometry
    • Equilibrium dialysis

    Main Results:

    • Cytidine 3'-phosphate discriminates between the enzyme's active sites.
    • Observed negative cooperativity at low ligand concentrations and positive cooperativity at high concentrations.
    • Ruled out hysteretic effects as the cause of non-hyperbolic kinetics.

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    Conclusions:

    • BS-RNAase displays mixed-type cooperativity in nucleotide binding.
    • A new model is proposed to explain the observed binding data.