Are you John Bosco Ahimbisibwe?

Claim your profile

Publications (2)1.79 Total impact

  • John Bosco Ahimbisibwe, Kousuke Inoue, Toshiyuki Shibata, Takahiko Aoki
    [Show abstract] [Hide abstract]
    ABSTRACT: The effect of bleeding on white muscle quality in amberjack and red sea bream was evaluated by measuring ATP-related compounds, volatile basic nitrogen (VBN), and the trimethylamine (TMA) content. The freshness was evaluated by the K value, and the degree of spoilage was elucidated by VBN and TMA. ATP was rapidly converted to ADP and AMP in the muscle and IMP was the main product of ATP degradation during iced storage. For both species, the IMP content was higher in the muscles of fish that were bled than in those unbled during iced storage. Conversely, the K value and the levels of hypoxanthine (Hx) and VBN were higher in the muscle tissue of unbled fish than in the bled tissue of both species. Similarly, the TMA content was higher in the unbled muscle tissues of both species after a week of storage. KeywordsBleeding-Fish muscle-IMP- K value-TMA-VBN
    Fisheries Science 03/2010; 76(2):389-394. · 0.90 Impact Factor
  • John Bosco Ahimbisibwe, Kousuke Inoue, Takahiko Aoki
    [Show abstract] [Hide abstract]
    ABSTRACT: Cathepsin L, one of the cysteine proteases found in fish muscle, is considered to be the main cause of post-mortem autolysis of fish muscle. We have determined the presence of cathepsin L in the membranes of red blood cells of carp, amberjack, and red sea bream and measured its activity. Immunoblotting of an extract of the red blood cell membranes from these three fish species using human anti-cathepsin L antibody revealed the presence of cathepsin L of different molecular masses. The molecular masses of cathepsin L was estimated to be 120 and 85kDa in the amberjack and 75 and 70kDa in the carp. These proteins have higher molecular masses than the mature form of cathepsin L, suggesting that they are precursor forms. In contrast, the protein in the red sea bream was estimated to have a molecular mass of 30kDa, suggesting that this cathepsin L is a mature form. The specific activity of cathepsin L was highest in the red blood cell membranes of the amberjack, followed by the carp and the red sea bream in descending order.
    Fisheries Science 76(1):155-159. · 0.90 Impact Factor