Steroid-protein interactions studied by fluorescence quenching

The results suggest that testosterone binding may alter bovine serum albumin conformation and that the measured binding capacity of this protein for testosterone is dependent on the protein concentration

Nicola A. Attallah; Gene F. Lata

2003

Scholarcy highlights

  • The procedure has been applied to systems containing androstane derivatives and proteins or aromatic amino acids. 2
  • The results suggest that testosterone binding may alter bovine serum albumin conformation and that the measured binding capacity of this protein for testosterone is dependent on the protein concentration
  • High molar ratios of bound steroid to protein are obtained with dilute albumin solutions and may reflect the N-F transformations observed by others
  • Binding of steroid to protein is modified by the presence and location of oxygen functions and double bonds

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