Purification and characterization of a long chain, fatty-acid-binding protein supplying the mitochondrial beta-oxidative system in the heart

Biochim Biophys Acta. 1978 Apr 26;533(2):457-64. doi: 10.1016/0005-2795(78)90391-4.

Abstract

A fatty-acid-binding protein with a molecular weight of approximately 12 000 was purified from rat heart and the binding investigated by electron spin resonance. The stearic acid bound to the protein was found to be transferred to the mitochondrial beta-oxidative system, suggesting a role as transcytoplasmic fatty acid carrier for this protein. For the first time a physiological cytoplasmic protein was used as a carrier supplying the mitochondrial beta-oxidative system. A new mechanism of action is proposed to explain the control exerted by this type of protein in some membrane-linked enzymatic processes.

MeSH terms

  • Animals
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Electron Spin Resonance Spectroscopy
  • Fatty Acids / metabolism*
  • Female
  • Mitochondria, Heart / metabolism*
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / metabolism*
  • Myocardium / metabolism*
  • Rats

Substances

  • Carrier Proteins
  • Fatty Acids
  • Muscle Proteins