Refolding and Reactivation of Escherichia coli Tryptophan Synthase β₂ Subunit after Inactivation and Dissociation in Guanidine Hydrochloride at Acidic pH

The Tryptophan Synthase from Escherichia coli

1975 • 131 citations

Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit

1970 • 110 citations

Kinetic aspects of conformational changes in proteins. II. Structural changes in renaturation of denatured proteins

1971 • 108 citations

Reassociation and Reactivation of Lactic Dehydrogenase from the Unfolded Subunits

1974 • 79 citations

Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme

1971 • 67 citations

Studies on protein subunits

1972 • 64 citations

Association of β-chain monomers of Escherichia coli tryptophan synthetase

1970 • 56 citations

Subunit structure of the B component of Escherichia coli tryptophan synthetase

1969 • 51 citations

Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli

1976 • 49 citations

Kinetic analysis of the reactivation of rabbit muscle aldolase after denaturation with guanidine·HCl

1977 • 30 citations

Ligand Binding to Enzyme Complexes

1975 • 16 citations

Equilibrium Studies and Kinetics of Reactivation, Refolding and Reassociation of Lactic Dehydrogenase and Glyceraldehyde-3- Phosphate Dehydrogenase

1977 • 12 citations