The requirements for activity of blue-green algal nitrogenase have been studied. The optimal concentration ranges for ATP and Na~S204 are 2--3 m~ and 4--10 mlYl respectively. A magnesium requirement has been confirmed but the enzyme is not specific for Mg ~+, Co 2+ and Mn 2+ will also support activi
Alanine dehydrogenase of the N2-fixing blue-green alga,Anabaena cylindrica
โ Scribed by P. Rowell; W. D. P. Stewart
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 1010 KB
- Volume
- 107
- Category
- Article
- ISSN
- 0302-8933
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โฆ Synopsis
The L-alanine dehydrogenase (ADH) of Anabaena cylindrica has been purified 700-fold. It has a molecular weight of approximately 270,000, has 6 sub-units, each of molecular weight approximately 43,000, and shows activity both in the aminating and deaminating directions. The enzyme is NADH/NAD+ specific and oxaloacetate can partially substitute for pyruvate. The Kampp for NAD+ is 14 muM and 60 muM at low and high NAD concentrations respectively.
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Anabaena cylindrica grown in steady state continuous culture has an extractable ATP pool, measured on the basis of the luciferin-luciferase assay of 165 +/- 35 nmoles ATP mg chla-1. This pool is maintained by a dynamic balance between the rate of ATP synthesis and the rate of ATP utilization. Phosph
In long-term experiments, nitrogen fixation in photosynthetic organisms is usually dependent upon the presence of light (FoGG and THAN TUN, 1960; F\_au and FOGG, 1962) although certain photosynthetic nitrogen-fixers can grow and fix nitrogen in the dark using organic media (Nostoc muscorum, ALLISON,