Interaction of muscle pyruvate kinase with 1,8-anilinonaphthalene sulfonate. |
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Authors: | K C Ingham C H Suelter |
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Affiliation: | Biochemistry Department, Michigan State University, East Lansing, Michigan 48824 USA |
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Abstract: | The interaction of the fluorescent probe 1,8-anilinonaphthalene sulfonate with rabbit muscle pyruvate kinase is reported. Four moles of 1,8-anilinonaphthalene sulfonate interact per mole of the 4-subunit enzyme with a dissociation constant of 1.7 × 10?4m at 30 °. The interaction is not competitive with substrates ADP and phosphoenolpyruvate, with cations K+ and Mg2+, nor with effector phenylalanine. |
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