Library

Your search history is empty.
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1970-1974  (1)
  • Properties  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 98 (1974), S. 93-100 
    ISSN: 1432-072X
    Keywords: Azotobacter ; Nitrogenase ; Iron Sulfur Proteins ; Properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...