Bovine skeletal muscle adenosine deaminase purification and some properties

1. 1. A low molecular weight form of adenosine deaminase from bovine skeletal muscle was purified about 930-fold. 2. 2. The enzyme had a mol. wt of 31,000, a K m value for adenosine of 2.37 × 10 −5M and a pH optimum at 7.0. 3. 3. This enzyme is very resistant to heat inactivation and does not requir...

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Veröffentlicht in:International journal of biochemistry 1984, Vol.16 (12), p.1279-1282
Hauptverfasser: Martinez, C., Zumalacarregui, J.M., Diez, V., Burgos, J.
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Sprache:eng
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Zusammenfassung:1. 1. A low molecular weight form of adenosine deaminase from bovine skeletal muscle was purified about 930-fold. 2. 2. The enzyme had a mol. wt of 31,000, a K m value for adenosine of 2.37 × 10 −5M and a pH optimum at 7.0. 3. 3. This enzyme is very resistant to heat inactivation and does not require metal activators or other dialysable cofactors. 4. 4. A possible role in the post-mortem metabolism of adenine nucleotide in skeletal muscle is discussed.
ISSN:0020-711X
DOI:10.1016/0020-711X(84)90228-3