Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin

Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin

Cleavage of natural inhibitor of mitochondrial ATPase by thrombin occurs at two specific sites. First an Arg-Ser bond is split giving two peptides. The main peptide which retains integral biological activity is further cleaved at two successive Arg-Ala bonds, none of the products is able to inhibit...

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Veröffentlicht in:Biochemical and biophysical research communications 1982-07, Vol.107 (2), p.435-441
Hauptverfasser: Dianoux, A.-C., Freyssinet, J.-M.
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphatases - antagonists & inhibitors
adenosinetriphosphatase inhibitor
Amino Acid Sequence
Animals
ATPase Inhibitory Protein
Cattle
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Horses
Humans
Mitochondria, Heart - analysis
Molecular Weight
Peptide Fragments - analysis
Proteins - metabolism
thrombin
Thrombin - pharmacology
Time Factors
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Beschreibung
Zusammenfassung:Cleavage of natural inhibitor of mitochondrial ATPase by thrombin occurs at two specific sites. First an Arg-Ser bond is split giving two peptides. The main peptide which retains integral biological activity is further cleaved at two successive Arg-Ala bonds, none of the products is able to inhibit ATPase. The isolation of these peptides and their characterization are described.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(82)91510-8