Determination of the primary structure of Paim II, an alpha-amylase inhibitor from Streptomyces coruchorushii, by high-performance tandem mass spectrometry
Akashi, S.; Hirayama, K.; Murai, A.; Arai, M.; Murao, S.
Biochemical and Biophysical Research Communications 158(2): 514-519
1989
ISSN/ISBN: 0006-291X PMID: 2783847 Document Number: 332574
This study indicates one of the advantages of tandem mass spectrometry; the primary structures of proteins with little structural difference can be determined by using tandem mass spectrometry without prior purification of each component. The primary structure of Paim II, a protein .alpha.-amylase inhibitor from Streptomyces coruchorushii, was determined by using tandem mass spectrometry. Paim II consists of two component proteins with ragged N-terminus, and was sequenced on the basis of the structure of Paim I, an analogous .alpha.-amylase inhibitor from the same natural origin.