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Isolation and amino acid sequence of a novel 6.8‐kDa mitochondrial proteolipid from beef heart
Author(s) -
Terzi E.,
Boyot P.,
Van Dorsselaer A.,
Luu B.,
Trifilieff E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80082-t
Subject(s) - cyanogen bromide , polyclonal antibodies , chemistry , fast atom bombardment , peptide sequence , protein primary structure , amino acid , biochemistry , molecular mass , mass spectrometry , chromatography , microbiology and biotechnology , antibody , biology , enzyme , immunology , gene
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/z 6834.1). 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.