𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Degradation of the nitrogenase proteins during encystment ofAzotobacter vinelandii

✍ Scribed by Werner Kössler; Diethelm Kleiner

Publisher
Springer
Year
1986
Tongue
English
Weight
467 KB
Volume
145
Category
Article
ISSN
0302-8933

No coin nor oath required. For personal study only.

✦ Synopsis

Nitrogenase activity in cell-free extracts of Azotobacter vinelandii declines during encystment. Upon germination a rapid increase in activity is observed, which is suppressed by rifampicin, suggesting that de novo biosynthesis of the nitrogenase proteins is required. The decline of activity during encystment is accompanied by disappearance of both nitrogenase proteins from cell extracts, indicating irreversible proteolysis. Total proteinase activity does not change significantly during encystment.

📜 SIMILAR VOLUMES

Physical and chemical properties of the
Physical and chemical properties of the nitrogenase proteins fromAzotobacter vinelandii
✍ D. Kleiner; C. H. Chen 📂 Article 📅 1974 🏛 Springer 🌐 English ⚖ 570 KB

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

Characterization of the gene for the Fe-
Characterization of the gene for the Fe-protein of the vanadium dependent alternative nitrogenase of Azotobacter vinelandii and construction of a Tn5 mutant
✍ Raina, Ramesh ;Reddy, M. Amarender ;Ghosal, Debabrota ;Das, H. K. 📂 Article 📅 1988 🏛 Springer 🌐 English ⚖ 762 KB

A sequence homologous to the conventional nifH gene has been cloned from a different region of the Azotobacter vinelandii genome. Tn5 insertions were obtained in this clone and the mutagenized plasmid was used for marker exchange with A. vinelandii strain CA12 (delta nifHDK) to obtain Tn5 mutants. T