Literature DB >> 6839713

The characterization of an adenosine deaminase from chicken serum.

A A Rokosu.   

Abstract

1. Adenosine deaminase from chicken serum was purified and characterized. 2. The Km and Vmax values of the enzyme in respect of adenosine as substrate were 7.14 x 10(-3) M and 8.5 microM/min respectively. AMP, ADP & ATP are poorly metabolized respectively in decreasing order. 3. The enzyme had no NADase and NADPase activities but the presence of either NAD or NADP in normal incubation mixture activated the enzyme. 4. Metal ions Zn2+, Ca2+ and Mg2+ activated the enzyme to various levels. 5. Some compounds, mercaptoethanol, dithiothreitol (DTT), dithiobisnitrobenzoate (DTNB) inhibited the enzyme to various extents.

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Year:  1983        PMID: 6839713     DOI: 10.1016/0305-0491(83)90207-9

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  The role of divalent cations in structure and function of murine adenosine deaminase.

Authors:  B F Cooper; V Sideraki; D K Wilson; D Y Dominguez; S W Clark; F A Quiocho; F B Rudolph
Journal:  Protein Sci       Date:  1997-05       Impact factor: 6.725

2.  Human ADA2 belongs to a new family of growth factors with adenosine deaminase activity.

Authors:  Andrey V Zavialov; Ake Engström
Journal:  Biochem J       Date:  2005-10-01       Impact factor: 3.857

  2 in total

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