Determination of the primary structure of Paim II, an alpha-amylase inhibitor from Streptomyces coruchorushii, by high-performance tandem mass spectrometry.
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.
Akashi
S
S
Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.
Hirayama
K
K
Murai
A
A
Arai
M
M
Murao
S
S
D000595:Amino Acid Sequence; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides; D013302:Streptomyces / Q000201:enzymology*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D010455:Peptides; D000516:alpha-Amylases