Abstract
Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.
Original language | English (US) |
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Pages (from-to) | 901-906 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 82 |
Issue number | 3 |
DOIs | |
State | Published - Jun 14 1978 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology