Isolation and amino acid sequence of a novel 6.8‐kDa mitochondrial proteolipid from beef heart

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 comp...

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Bibliographic Details
Published inFEBS letters Vol. 260; no. 1; pp. 122 - 126
Main Authors Terzi, E., Boyot, P., Van Dorsselaer, A., Luu, B., Trifilieff, E.
Format Journal Article
LanguageEnglish
Published 15.01.1990
Subjects
Amino acid sequence
Bovine heart
Fast atom bombardment-mass spectrometry
Mitochondria
Proteolipid
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)80082-T