In rats, acetylcholinesterase (AChE) activity in the fast muscles is several times higher than in the slow soleus muscle. The hypothesis that specific neural impulse patterns in fast or slow muscles are responsible for different AChE activities was tested by altering the neural activation pattern in
Activities of phospholipases A and lysophospholipases in glycolytic and oxidative skeletal muscles in the rabbit
โ Scribed by Alasnier, Corinne; Gandemer, Gilles
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 111 KB
- Volume
- 80
- Category
- Article
- ISSN
- 0022-5142
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โฆ Synopsis
Oxidative muscles contain more free fatty acids than glycolytic muscles, which could explain in part their higher sensitivity to oxidation. These fatty acids are partly the result of phospholipid hydrolysis catalysed by phospholipases A and lysophospholipases. Up to now, very little is known on the activities of these enzymes in skeletal muscles. This study deals with the activities of phospholipases A and lysophospholipases in ยฎve rabbit muscles covering a large range of metabolic types (oxidative Soleus and Semimembranosus proprius muscles, glycolytic Psoas major and Longissimus lumborum muscles and intermediate Gastrocnemius laterale muscle). The results showed that (a) phospholipases A and lysophospholipases had maximal activity at pH 8ยฑ9; (b) phospholipases A and lysophospholipases retained more than 50% of their maximal activity at pH 5.5ยฑ6, the ultimate pH of muscles; (c) lysophospholipases exhibited a higher activity than phospholipases A (4ยฑ7-fold higher in the oxidative muscles, 11-fold higher in the intermediate muscle and 18ยฑ23-fold higher in the glycolytic muscles); and (d) phospholipase A and lysophospholipase activities were higher in oxidative muscles than in glycolytic muscles (10ยฑ25-fold higher for phospholipases A and 4ยฑ5-fold higher for lysophospholipases). Thus oxidative muscles have a higher potential activity for post-mortem hydrolysis of phospholipids.
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