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1999 (1)
1Author    Toshiro Matsui, Tomoyuki Oki, Yutaka OsajimaRequires cookie*
 Title    Isolation and Identification of Peptidic a-Glucosidase Inhibitors Derived from Sardine Muscle Hydrolyzate  
 Abstract    We report here the isolation of a-glucosidase (A G H) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alka­ line protease. A s a result of reversed-phase HPLC purification, two A G H inhibitory peptides were isolated from a D EA E -Sephadex A-25 column eluate. The peptides were identified as follows: V al-Trp (IC50 = 22.6 mM) and T ry -T y r -P r o -L e u (IC50 = 3.7 mM). A G H inhibitory studies of T r y -T y r -P r o -L e u and its derivatives demonstrated the importance of the tri­ peptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity. 
  Reference    Z. Naturforsch. 54c, 259 (1999); received August 25/October 5 1998 
  Published    1999 
  Keywords    a-G lucosidase Inhibition, Diabetes, Sardine Muscle Hydrolyzate, Peptide 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0259.pdf 
 Identifier    ZNC-1999-54c-0259 
 Volume    54