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 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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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. |
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ISSN: | 0020-711X |
DOI: | 10.1016/0020-711X(84)90228-3 |