Isolation and amino acid sequence of a novel 6.8-kDa mitochondrial proteolipid from beef heart. Use of FAB-MS for molecular mass determination

FEBS Lett. 1990 Jan 15;260(1):122-6. doi: 10.1016/0014-5793(90)80082-t.

Abstract

We have isolated a 6.8 kDa proteolipid from an acidic chloroform/methanol extract of bovine cardiac muscle. The molecular mass of the polypeptide was measured by fast atom bombardment-mass spectrometry (FAB-MS) (m/z6834.1). Its amino acid sequence was partly determined by direct sequencing and completed by characterization of cyanogen bromide and tryptic fragments (sequencing, FAB-MS and amino acid analysis). The polypeptide consists of 60 amino acid residues. Polyclonal antibodies raised in rabbit allowed its localization by electroimmunoblotting in mitochondria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Immunoblotting
  • Mass Spectrometry
  • Mitochondria, Heart / analysis*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / isolation & purification
  • Peptides / isolation & purification
  • Proteolipids / isolation & purification*
  • Solvents

Substances

  • Peptide Fragments
  • Peptides
  • Proteolipids
  • Solvents

Associated data

  • GENBANK/Y07527