These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: High activities of cathepsins B, D, H, and L in the white muscle of chum salmon in spawning migration.
    Author: Yamashita M, Konagaya S.
    Journal: Comp Biochem Physiol B; 1990; 95(1):149-52. PubMed ID: 2331869.
    Abstract:
    1. Activities of cathepsins, lysosomal hydrolytic enzymes and cysteine protease inhibitor in both the white and red muscles of chum salmon (Oncorhynchus keta) caught during spawning and feeding migrations were compared. 2. In the white muscle, cathepsins B, D, H and L activities were 3-7 times higher in the fish in spawning migration than those in feeding migration. However, in the red muscle, no such marked differences were observed between them. 3. Cysteine protease inhibitory activity and extractable protein content in the white muscle of the fish in spawning migration were about 40% lower than those in feeding migration. 4. The present study supports the conception that the cathepsins are related to protein catabolism of the fish during spawning migration.
    [Abstract] [Full Text] [Related] [New Search]