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Bovine skeletal muscle adenosine deaminase. Purification and some properties.

作者信息

Martinez C, Zumalacarregui J M, Diez V, Burgos J

出版信息

Int J Biochem. 1984;16(12):1279-82. doi: 10.1016/0020-711x(84)90228-3.

Abstract

A low molecular weight form of adenosine deaminase from bovine skeletal muscle was purified about 930-fold. The enzyme had a mol. wt of 31,000, a Km value for adenosine of 2.37 X 10(-5) M and a pH optimum at 7.0. This enzyme is very resistant to heat inactivation and does not require metal activators or other dialysable cofactors. A possible role in the post-mortem metabolism of adenine nucleotide in skeletal muscle is discussed.

摘要

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