Sarcomeric disorganization in post-mortem fish muscles.
1. The post-mortem evolution of protein pattern in fish striated muscle was followed by SDS-PAGE, after different conditions of storage time and temperature. 2. Sarcoplasmic and sarcomeric fractions were analyzed respectively by low and high ionic strength extractions of fish muscle samples. 3. No evident modification of electrophoretic patterns was observed during the pre-rigor mortis period. 4. The high mol. wt proteins titin and nebulin were highly sensitive to proteolysis during the rigor mortis period. 5. Myosin extraction was predominantly influenced by the storage temperature. The myosin content of the extracts decreased during the rigor mortis period at storage temperatures greater than 8 degrees C. 6. alpha-Actinin was very resistant to proteolysis, but could be released from Z-disc structure during post-mortem aging.
Astier
C
C
Centre de Recherches de Biochimie Macromoléculaire (C.N.R.S.), Unité 249 (I.N.S.E.R.M.), Montpellier, France.
Labbe
J P
JP
Roustan
C
C
Benyamin
Y
Y
D000185:Actinin / Q000378:metabolism; D000818:Animals; D064211:Connectin; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes; D007700:Kinetics; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D011180:Postmortem Changes; D011494:Protein Kinases; D012518:Sarcomeres / Q000378:metabolism*; D013696:Temperature; D014335:Tropomyosin / Q000378:metabolism
D064211:Connectin; D009124:Muscle Proteins; D014335:Tropomyosin; C035620:nebulin; D000185:Actinin; D011494:Protein Kinases; D009218:Myosins