Issue 13, 1977

Detection of enzyme-bound intermediates by cross-saturation in nuclear magnetic resonance spectroscopy; an investigation of the papain–N-benzoylaminoacetaldehyde complex

Abstract

A hemithioacetal formed between the active site thiol of the proteolytic enzyme papain, and the inhibitor N-benzoylaminoacetaldehyde, has been detected by a double resonance experiment in which magnetisation is transferred between the enzyme-bound and free inhibitor.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1977, 451-453

Detection of enzyme-bound intermediates by cross-saturation in nuclear magnetic resonance spectroscopy; an investigation of the papain–N-benzoylaminoacetaldehyde complex

P. I. Clark, G. Lowe and D. Nurse, J. Chem. Soc., Chem. Commun., 1977, 451 DOI: 10.1039/C39770000451

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