Abstract
The purified Mo-Fe protein and Fe protein of nitrogenase from Azotobacter vinelandii have molecular weights (MW) of about 216000 and 64000, respectively. The Mo-Fe protein is composed of subunits of about 56000 MW, and the Fe protein has 2 equivalent subunits of about 33000 MW. The isoelectric point of the Mo-Fe protein is 5.2 and that of the Fe protein is 4.7. Amino acid compositions reflect the acidic nature of the proteins. The Mo-Fe protein yielded 24 atoms of Fe, 20 atoms of acid-labile sulfide and 1.54 atoms of Mo per molecule. Analysis of the Fe protein showed 3.45 atoms of Fe per molecule.
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Abbreviations
- MW:
-
molecular weight
- SDS:
-
sodium dodecylsulfate
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Kleiner, D., Chen, C.H. Physical and chemical properties of the nitrogenase proteins from Azotobacter vinelandii . Arch. Microbiol. 98, 93–100 (1974). https://doi.org/10.1007/BF00425272
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DOI: https://doi.org/10.1007/BF00425272