I. Lorenzoni

Human erythrocyte glucose 6-phosphate dehydrogenase. Physical properties.

R. Cancedda, A. De Flora, A. Bonsignore, 1971, Biochemical and biophysical research communications.

Effect of divalent cations on the structure of human erythrocyte glucose 6-P dehydrogenase.

R. Cancedda, A. De Flora, A. Bonsignore, 1971, Biochemical and biophysical research communications.

Distinctive patterns of NADP binding to dimeric and tetrameric glucose 6-phosphate dehydrogenase from human red cells.

R. Cancedda, A. De Flora, A. Bonsignore, 1970, Biochemical and biophysical research communications.

A new hepatic protein inactivating glucose 6-phosphate dehydrogenase.

A. De Flora, A. Bonsignore, S. Alemà, 1968, The Biochemical journal.

Electrophoretic behaviour of human erythrocyte glucose 6-phosphate dehydrogenase during purification.

A. De Flora, A. Bonsignore, D. Dina, 1968, Biochemical and biophysical research communications.

Purification of glucose 6-phosphate dehydrogenase from human erythrocytes.

R. Cancedda, A. De Flora, A. Bonsignore, 1970, The Italian journal of biochemistry.

Metabolism of human erythrocyte glucose 6-phosphate dehydrogenase. V. Exchange between free and apoenzyme-bound NADP.

R. Cancedda, A. De Flora, A. Morelli, 1969, The Italian journal of biochemistry.

Metabolism of human erythrocyte glucose‐6‐phosphate dehydrogenase. III ‐ isolation of a protein involved in the 6‐phosphogluconate‐induced inactivation

R. Cancedda, A. De Flora, A. Bonsignore, 1968, FEBS letters.