Denaturation mode of carp myofibrils when affected by temperature and salt concentration

Fisheries Science

Volumn 68, Issue 3, 2002, Pages 627-633

  Yamamoto, Takeshi ^a   Takahashi, Masayuki ^a   Kato, Sanae ^a,b   Konno, Kunihiko ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b ASAHIKAWA MEDICAL COLLEGE   (Japan)

Author keywords

Aggregation; Gelation; Myofibrils; Myosin; Salt solubility; Thermal denaturation

Indexed keywords

CYPRINUS CARPIO;

EID: 0036311046     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1444-2906.2002.00470.x     Document Type: Article

References (14)

1. Thermostability of fish myofibrillar Ca-ATPase and adaptation to environmental temperature
2. The effect of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish
3. cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature
4. A new method for evaluation of the quality of frozen surimi from Alaska pollack: Relationship between myofibrillar ATPase activity and Kamaboko forming ability of frozen surimi
5. Isolation of carp myosin rod and its structural stability
6. Thermal unfolding of myosin rod and light meromyosin: Circular dichroism and tryptophan fluorescence studies
7. Early structural changes in myosin rod upon heating of carp myofibrils
8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
9. Mg-ATPase activity enhancement of carp myofibrils upon thermal treatment
10. Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry
11. Solubilization of fish muscle myosin by sorbitol
12. Structural changes of carp myosin subfragment-1 induced by thermal denaturation
13. Oligomerization of carp myosin which retains its ATPase activity
14. Freeze denaturation of carp myofibrils compared with thermal denaturation