Binding of the Recombinant Proteinase Inhibitor Eglin c, of the Soybean Bowman-Birk Proteinase Inhibitor and of its Chymotrypsin and Trypsin Inhibiting Fragments to Leu-Proteinase, the Leucine Specific Serine Proteinase from Spinach (Spinacia oleracea L.) Leaves: Thermodynamic Study

Paolo Ascenzi C.N.R., Center for Molecular Biology, Department of Biochemical Sciences, University of Rome “La Sapienza”, Piazzale Aldo Moro 5, 00185, Rome, Italy

Gino Amiconi C.N.R., Center for Molecular Biology, Department of Biochemical Sciences, University of Rome “La Sapienza”, Piazzale Aldo Moro 5, 00185, Rome, Italy

Alessandro Ballio C.N.R., Center for Molecular Biology, Department of Biochemical Sciences, University of Rome “La Sapienza”, Piazzale Aldo Moro 5, 00185, Rome, Italy

Martino Bolognesi Department of Genetics and Microbiology, Section of Crystallography, University of Pavia, Via Taramelli 16, 27100, Pavia, Italy

Enea Menegatti Department of Pharmaceutical Sciences, University of Ferrara, Via Scandiana 21, 44100, Ferrara, Italy

Hans Peter Schnebli Pharma Research, Ciba-Geigy AG, Postfach, CH-4002, Basel, Switzerland

Patrizia Aducci Department of Biology, University of Rome “Tor Vergata”, Via Orazio Raimondo, 8, 00173, Rome, Italy

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Binding of the Recombinant Proteinase Inhibitor Eglin c, of the Soybean Bowman-Birk Proteinase Inhibitor and of its Chymotrypsin and Trypsin Inhibiting Fragments to Leu-Proteinase, the Leucine Specific Serine Proteinase from Spinach (Spinacia oleracea L.) Leaves: Thermodynamic Study

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Binding of the Recombinant Proteinase Inhibitor Eglin c, of the Soybean Bowman-Birk Proteinase Inhibitor and of its Chymotrypsin and Trypsin Inhibiting Fragments to Leu-Proteinase, the Leucine Specific Serine Proteinase from Spinach (Spinacia oleracea L.) Leaves: Thermodynamic Study

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