Isolation and Partial Characterization of Het − Fix − Mutant Strain of the Diazotrophic Cyanobacterium Anabaena variabilis Showing Chromatic Adaptation

2001 ◽  
Vol 43 (4) ◽  
pp. 265-270 ◽  
Author(s):  
Bhanumati Singh ◽  
Vinay S. Chauhan ◽  
Surendra Singh ◽  
Prakash S. Bisen
Keyword(s):  
Mutant Strain ◽  
Anabaena Variabilis ◽  
Chromatic Adaptation ◽  
Partial Characterization ◽  
Cyanobacterium Anabaena

Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis

1994 ◽  
Vol 49 (1-2) ◽  
pp. 70-78 ◽  
Author(s):  
Ulrike Strohmeier ◽  
Christian Gerdes ◽  
Wolfgang Lockau
Keyword(s):  
Ion Exchange ◽  
Proteolytic Enzymes ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Anabaena Variabilis ◽  
Prolyl Endopeptidase ◽  
Cyanobacterium Anabaena

Soluble extracts of the cyanobacterium Anabaena variabilis ATCC 29413 and an engineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion exchange chromatography, and protease profiles determined using azocasein, Nα-benzoyl-ᴅ,ʟ arginine- 4-nitroanilide and N-carbobenzoxy-glycyl-ʟ-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopeptidase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm.

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