Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442-, and Val561-plasmin: a comparative study.

Biochimica et biophysica acta - 1 Aug 1990

Ascenzi P, Amiconi G, Bolognesi M, Menegatti E, Guarneri M

Abstract excerpt

Thermodynamic and kinetic parameters for the binding of the bovine basic pancreatic trypsin inhibitor (BPTI, Kunitz inhibitor) to human Glu1-, Lys77-, Val442- and Val561-plasmin (EC 3.4.21.7) have been determined between pH 3.0 and 9.5, and from 5.0 to 45.0 degrees C. The inhibitor-binding properties to human Glu1-, Lys77-, Val442- and Val561-plasmin suggest a possible role of BPTI in modulating plasmin activity...

Topics

Fibrinolysin
Glutamine
Humans
Hydrogen-Ion Concentration
Kinetics
Lysine
Mutation
Protein Binding
Recombinant Proteins
Thermodynamics
Trypsin Inhibitor, Kunitz Soybean

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Trypsin Inhibitors

Valine

Source

Identifiers

PMID: 2143086
DOI: 10.1016/0167-4838(90)90157-b

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2143086-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442-, and Val561-plasmin: a comparative study.PMID 2143086Read ↗

Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases.Semantic proximity Read ↗

Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).Semantic proximity Read ↗

Structural studies of the interactions of normal and abnormal human plasmins with bovine basic pancreatic trypsin inhibitor.Semantic proximity Read ↗

Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2.Semantic proximity Read ↗

Distal hinge of plasminogen activator inhibitor-1 involves its latency transition and specificities toward serine proteases.Semantic proximity Read ↗

Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor.Semantic proximity Read ↗

The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity.Semantic proximity Read ↗

Structure of BbKI, a disulfide-free plasma kallikrein inhibitor.Semantic proximity Read ↗

The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI.Semantic proximity Read ↗

Effect of phospholipids on conformational structure of bovine pancreatic trypsin inhibitor (BPTI) and its thermolabile mutants.Semantic proximity Read ↗

Importance of the hinge region between alpha-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neutralizing antibodies.Semantic proximity Read ↗

Phage display selection of P1 mutants of BPTI directed against five different serine proteinases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.