Binding of the bovine pancreatic secretory trypsin inhibitor (Kazal) to bovine serine (pro)enzymes

Enea Menegatti, Mario Guarneri, Martino Bolognesi, Paolo Ascenzi, Gino Amiconi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The effect of temperature and pH on the association equilibrium constant (Ka) for the binding of the bovine pancreatic secretory trypsin inhibitor (bovine PSTI, type I; Kazal inhibitor) to bovine β-trypsin, bovine α-chymotrypsin and bovine trypsinogen has been investigated. The results suggest that serine (pro)enzyme inhibitor interaction involves both rigorous spatial configuration and molecular flexibility.

Original languageEnglish
Pages (from-to)129-132
Number of pages4
JournalJournal of Molecular Biology
Volume198
Issue number1
DOIs
Publication statusPublished - Nov 5 1987

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Kazal Pancreatic Trypsin Inhibitor
Aprotinin
Serine
Enzymes
Trypsinogen
Molecular Conformation
Enzyme Inhibitors
Temperature

ASJC Scopus subject areas

  • Virology

Cite this

Binding of the bovine pancreatic secretory trypsin inhibitor (Kazal) to bovine serine (pro)enzymes. / Menegatti, Enea; Guarneri, Mario; Bolognesi, Martino; Ascenzi, Paolo; Amiconi, Gino.

In: Journal of Molecular Biology, Vol. 198, No. 1, 05.11.1987, p. 129-132.

Research output: Contribution to journalArticle

Menegatti, Enea ; Guarneri, Mario ; Bolognesi, Martino ; Ascenzi, Paolo ; Amiconi, Gino. / Binding of the bovine pancreatic secretory trypsin inhibitor (Kazal) to bovine serine (pro)enzymes. In: Journal of Molecular Biology. 1987 ; Vol. 198, No. 1. pp. 129-132.
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