The primary structure of alpha-amylase inhibitor Z-2685 from Streptomyces parvullus FH-1641. Sequence homology between inhibitor and alpha-amylase.

@article{Hofmann1985ThePS,
  title={The primary structure of alpha-amylase inhibitor Z-2685 from Streptomyces parvullus FH-1641. Sequence homology between inhibitor and alpha-amylase.},
  author={Olaf Hofmann and L{\'a}szl{\'o} V{\'e}rtesy and Gerhard Braunitzer},
  journal={Biological chemistry Hoppe-Seyler},
  year={1985},
  volume={366 12},
  pages={1161-8}
}
The native and oxidized alpha-amylase inhibitor Z-2685, isolated from the culture medium of Streptomyces parvullus FH-1641, and its overlapping cleavage products were degraded by the automatic Edman technique. Digestion was carried out with pepsin, thermolysin and trypsin. The alpha-amylase inhibitor is a polypeptide consisting of 76 amino acids with a molecular mass of 8 129 Da. With the exception of methionine and lysine, all naturally occurring amino acids are present. It is interesting that… CONTINUE READING