Mass spectral identification of the blocked N‐terminal tryptic peptide of the ATPase inhibitor from beef heart mitochondria
Open Access
- 20 August 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 174 (1), 151-156
- https://doi.org/10.1016/0014-5793(84)81095-9
Abstract
The presence of a formyl blocking group at the N‐terminus of the ATPase inhibitor has been identified and the partial sequence of the N‐terminal peptide has been determined by fast atom bombardment and field desorption coupled to mass spectrometry. Minor discrepancies in amino acid sequence of the inhibitor between the present and published data [(1981) Proc. Natl. Acad. Sci. USA 78, 7403‐7407] are reported and its relationships with other inhbitors are briefly discussed.Keywords
This publication has 24 references indexed in Scilit:
- Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombinBiochemical and Biophysical Research Communications, 1982
- The amino acid sequence of toxin V from Anemonia sulcataBiochemical and Biophysical Research Communications, 1982
- Effects of proteolytic fragmentations on the activity of the mitochondrial natural ATPase inhibitorFEBS Letters, 1982
- Exopeptidase digestion in combination with field desorption mass spectrometry for amino acid sequence determinationFEBS Letters, 1982
- Partial proteolysis of the natural ATPase inhibitor from beef heart mitochondriaFEBS Letters, 1981
- Photoaffinity labeling of mitochondrial adenosine triphosphatase by an azido derivative of the natural adenosine triphosphatase inhibitorBiochemistry, 1981
- Characterization of the morphogenesis-dependent cleavage region of the major capsid protein (P23) of bacteriophage T4; sequence of an amber fragment of P23Journal of Molecular Biology, 1978
- Determination of the complete amino acid sequence of bovine cardiac troponin CBiochemistry, 1976
- ATPase inhibitor from yeast mitochondria. Purification and propertiesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- The equilibrium between the mitochondrial ATPase (F1) and its natural inhibitor in submitochondrial particlesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974