Issue 17, 1995

The role of papain in the association process of a 1-pyrenoyl pendant attached to its active site

Abstract

An analysis of the spectroscopic behaviour of papain modified by 1-bromoacetylpyrene demonstrates that the active site of this enzyme remarkably promotes the formation of the ground-state dimer derived from the pyrenoyl pendant covalently bound to the cysteine-25 residue.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1995, 1729-1730

The role of papain in the association process of a 1-pyrenoyl pendant attached to its active site

T. Sakurai, K. Watanabe, K. Nojima and H. Inoue, J. Chem. Soc., Chem. Commun., 1995, 1729 DOI: 10.1039/C39950001729

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