English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Myosins and their rod fragments from fast skeletal muscles of carp acclimated to 10 and 30•Ž were digested with ƒ¿-chymotrypsin. Myosins in 0.12 M NaCl were digested at 10•Ž with the protease at an en zyme-to-myosin weight ratio of 1 / 100 which cleaved mainly the region connecting myosin subfragm ent-l and rod. When relative amounts of remaining myosin heavy chain band from the 10•Ž-acclimat ed carp were plotted on a logarithmic scale against reaction time, digestion was found to proceed in the first order reaction with 4.2 •~ 10-4 s-1, which was lower than 6.1 •~ 10-4 s-1 for the 30•Ž-acclimated carp (P<0.05). The other region, which is susceptible to protease and located between myosin subfrag ment-2 and light meromyosin, was examined at 10•Ž using myosin rod in 0.5 M KCl and ƒ¿-chymotryp sin with an enzyme-to-rod weight ratio of 1 / 120. Both myosin rods from the 10 and 30•Ž-acclimated carp gave about 2 •~ 10-4 s-1, with no differences in protease susceptibility. These results are in marked contrast to our previous observation that myosin from the 10•Ž-acclimated carp is less thermostable in the crossbridge head and a-helical region of the rod part than that from the 30•Ž-acclimated carp.

Protease Susceptibility of Fast Skeletal Myosin Heavy Chain form Carp Acclimated to Cold and Warm Tempratures