马肌肉中的AMP脱氨酶：纯化及调节特性的测定
AMP deaminase from equine muscle: purification and determination of regulatory properties.
作者信息
Raffin J P, Thebault M T
机构信息
Laboratoire de Biologie Marine du Collége de France, Concarneau.
出版信息
Int J Biochem. 1991;23(10):1069-78. doi: 10.1016/0020-711x(91)90147-f.
PMID:1786850
Abstract
- AMP deaminase from thoroughbred horse muscle was purified to apparent homogeneity and its regulatory properties were determined at pH 6.5 and 7.4. 2. The results are discussed in relation to the potential role of muscle AMP deaminase during exercise and the existence of two molecular forms depending on the pH.
摘要
- 对纯种马肌肉中的AMP脱氨酶进行了纯化，使其达到表观均一性，并在pH 6.5和7.4条件下测定了其调节特性。2. 结合运动过程中肌肉AMP脱氨酶的潜在作用以及取决于pH值的两种分子形式的存在对结果进行了讨论。
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