Functional domains of the ATPase inhibitor protein from bovine heart mitochondria

FEBS Lett. 2000 Sep 29;482(1-2):163-6. doi: 10.1016/s0014-5793(00)02055-x.

Abstract

A study is presented of the activity and temperature dependence of the ATPase inhibitor protein (IF(1)) from bovine heart mitochondria and of synthetic partial IF(1) peptides. The results show that the IF(1)-(42-58) peptide is the most potent inhibitory domain of IF(1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPase Inhibitory Protein
  • Adenosine Triphosphatases / antagonists & inhibitors*
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / isolation & purification
  • Intracellular Membranes / chemistry
  • Intracellular Membranes / metabolism
  • Kinetics
  • Mitochondria, Heart / chemistry
  • Mitochondria, Heart / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Fragments / pharmacology
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Thermodynamics

Substances

  • Enzyme Inhibitors
  • Peptide Fragments
  • Proteins
  • Adenosine Triphosphatases