Catalytic properties of bovine α-thrombin: a comparative steady-state and pre-steady-state study

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

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Abstract

Values of steady-state and pre-steady-state parameters for the bovine β-thrombin-catalyzed hydrolysis of ZArgONp and ZLysONp have been determined between pH 2.5 and 8 (I = 0.1 M) at 21 ± 0.5°C. Kinetic properties of bovine α-thrombin have been analyzed in parallel with those of porcine pancreatic β-kallikrein-B and bovine α-trypsin, all acting on cationic substrates. The different primary specificity and catalytic behaviour of these three serine proteinases reflect subtle structural differences at their S1 subsite, especially at residue positions 190, 221 and 226 as well as in the 217-219 segment.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume871
Issue number3
DOIs
Publication statusPublished - Jun 23 1986

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Keywords

  • (Bovine plasma)
  • pH effect
  • Proteinase kinetics
  • Substrate specificity
  • Thrombin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

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