Purification of Hydrogenase from Chlamydomonas reinhardtii
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چکیده
منابع مشابه
Purification of Hydrogenase from Chlamydomonas reinhardtii.
A method is described which results in a 2750-fold purification of hydrogenase from Chlamydomonas reinhardtii, yielding a preparation which is approximately 40% pure. With a saturating amount of ferredoxin as the electron mediator, the specific activity of pure enzyme was calculated to be 1800 micromoles H(2) produced per milligram protein per minute. The molecular weight was determined to be 4...
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The eukaryotic green alga, Chlamydomonas reinhardtii, produces H(2) under anaerobic conditions, in a reaction catalysed by an [FeFe]-hydrogenase. To identify genes that influence H(2) production in C. reinhardtii, a library of 6000 colonies on agar plates was screened with sensitive chemochromic H(2)-sensor films for clones defective in H(2) production. Two mutants of particular interest were f...
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NAD-isocitrate dehydrogenase (NAD-IDH) from the eukaryotic microalga Chlamydomonas reinhardtii was purified to electrophoretic homogeneity by successive chromatography steps on Phenyl-Sepharose, Blue-Sepharose, diethylaminoethyl-Sephacel, and Sephacryl S-300 (all Pharmacia Biotech). The 320-kD enzyme was found to be an octamer composed of 45-kD subunits. The presence of isocitrate plus Mn2+ pro...
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Mitochondria were isolated from autotrophically grown Chlamydomonas reinhardtii cell-wall-less mutant CW 92. The cells were broken by vortexing with glass beads, and the mitochondria were collected by differential centrifugation and purified on a Percoll gradient. The isolated mitochondria oxidized malate, pyruvate, succinate, NADH, and [alpha]-ketoglutarate. Respiratory control was obtained wi...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1984
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.75.3.705