SARCOMERIC DISORGANIZATION IN POSTMORTEM FISH MUSCLES

被引：30

作者：

ASTIER, C ^{[1
]}

LABBE, JP ^{[1
]}

ROUSTAN, C ^{[1
]}

BENYAMIN, Y ^{[1
]}

机构：

[1] UNIV MONTPELLIER 1,CTR RECH BIOCHIM MACROMOLEC,CNRS,LP 8402,INSERM,U249,F-34033 MONTPELLIER,FRANCE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1991年 / 100卷 / 03期

关键词：

D O I：

10.1016/0305-0491(91)90204-Q

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：459 / 465

页数：7

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