Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10541789 | Food Chemistry | 2011 | 9 Pages |
Abstract
Soft textured Atlantic salmon is a sporadic and occasionally very severe problem for the farming and processing industries. The firm and soft fillets examined in this work differed in their gelatinase activities, cross-reactivity with anti-ubiquitin and anti-cathepsin L antibodies, as well as in the in-gel α-chymotryptic peptide maps of electrophoretically isolated myosin heavy chain (MHC) bands. The immunodetections of actin, α-actinin, MHC, and the MALDI TOF MS peptide mass fingerprinting of electrophoretically isolated MHCs only showed minor differences between samples. Other analyses revealed merely individual differences. These results seem to indicate a higher level of gelatinase activation, ubiquitination and cathepsin L cross-reacting material in softer muscle. These results would be consistent with a myopathy, but also with what could be expected in the skeletal muscle of healthy salmonid fish during a normal period of hyperplastic growth.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Iciar Martinez, PÃ¥l Anders Wang, Rasa Slizyté, Alberto Jorge, Stine W. Dahle, Benito Cañas, Michiaki Yamashita, Ragnar L. Olsen, Ulf Erikson,